Ubiquitin-lytic peptide fusion gene constructs, protein products deriving therefrom, and methods of making and using same

ABSTRACT

Stabilized ubiquitin-lytic peptide fusion polypeptides and a method of making the same by sub-cloning nucleic acid sequences coding for lytic peptides into a plasmid vector comprising a promoter and ubiquitin polypeptide coding sequence, wherein the ubiquitin polypeptide sequence is linked to the 5&#39; end of the lytic peptide nucleic acid sequence and is translated as a fusion polypeptide.

CROSS REFERENCE TO RELATED APPLICATIONS

This is a divisional of application Ser. No. 08/279,472, filed Jul. 22,1994, now abandoned, which is a continuation-in-part of Application No.08/231,730, filed April 20, 1994, now abandoned, in the names of JesseM. Jaynes and Gordon R. Julian, which in turn is a continuation-in-partof Application No. 08/225,476, filed Apr. 8, 1994, now abandoned, in thenames of Jesse M. Jaynes and Gordon R. Julian, which is in turn acontinuation-in-part of Application No. 08/148,491, filed Nov. 8, 1993,now abandoned, and Application No. 08/148,889, filed Nov. 8, 1993, nowabandoned, both filed in the name of Gordon R. Julian, which are in turncontinuation-in-part of Application No. 08/039,620, filed Jun. 4, 1993,now abandoned, in the name of Jesse M. Jaynes and Gordon R. Julian.

BACKGROUND OF THE INVENTION

1. Field of the Invention

The present invention relates to ubiquitin-lytic peptide fusion geneconstructs with enhanced stability and gene expression, ubiquitin-lyticpeptide fusion protein products, and methods of making and using thesame.

2. Description of Related Art

Naturally occurring lytic peptides play an important if not criticalrole as immunological agents in insects and have some, albeit secondary,defense functions in a range of other animals. The function of thesepeptides is to destroy procaryotic and other non-host cells bydisrupting the cell membrane and promoting cell lysis. Common featuresof these naturally occurring lytic peptides include an overall basiccharge, a small size (23-39 amino acid residues), and the ability toform amphipathic α-helices or β-pleated sheets. Several types of lyticpeptides have been identified: cecropins (described in U.S. Pat. Nos.4,355,104 and 4,520,016 to Hultmark et al.), defensins, sarcotoxins,melittin, and magainins (described in U.S. Patent No. 4,810,777 toZasloff). Each of these peptide types is distinguished by sequence andsecondary structure characteristics.

Several hypotheses have been suggested for the mechanism of action ofthe lytic peptides: disruption of the membrane lipid bilayer by theanphipathic α-helix portion of the lytic peptide; lytic peptideformation of ion channels, which results in osmotically inducedcytolysis; lytic peptide promotion of protein aggregation, which resultsin ion channel formation; and lytic peptide-induced release ofphospholipids. Whatever the mechanism of lytic peptide-induced membranedamage, an ordered secondary conformation such as an amphipathic α-helixand positive charge density are features that appear to participate inthe function of the lytic peptides.

Active synthetic analogs of naturally occurring lytic peptides have beenproduced and tested in vitro against a variety of procaryotic andeukaryotic cell types (see for example Arrowood, M. J., et al., J.Protozool. 38: 161s 199!; Jaynes, J. M., et al., FASEB J. 2: 28781988!), including: gram positive and gram negative bacteria, fungi,yeast, protozoa, envelope viruses, virus-infected eukaryotic cells, andneoplastic or transformed mammalian cells. The results from thesestudies indicate that many of the synthetic lytic peptide analogs havesimilar or higher levels of lytic activity for many different types ofcells, compared to the naturally occurring forms. In addition, thepeptide concentration required to lyse microbial pathogens such asprotozoans, yeast, and bacteria does not lyse normal mammalian cells.However, because previous work demonstrates that absolute sequence isnot important as long as positive charge and amphipathy are preserved,the level of activity for a given synthetic peptide is difficult topredict.

The specificity of the lytic action also depends upon the concentrationof the peptide and the type of membrane with which it interacts. Jaynes,J. M. et al., Peptide Research 2: 157 (1989) discuss the alteredcytoskeletal characteristics of transformed or neoplastic mammaliancells that make them susceptible to lysis by the peptides. In theseexperiments, normal, human non-transformed cells remained unaffected ata given peptide concentration while transformed cells were lysed;however, when normal cells were treated with the cytoskeletal inhibitorscytochalasin D or colchicine, sensitivity to lysis increased. Theexperiments show that the action of lytic peptides on normal mammaliancells is limited. This resistance to lysis was most probably due to thewell-developed cytoskeletal network of normal cells. In contrast,transformed cell lines which have well-known cytoskeletal deficiencieswere sensitive to lysis. Because of differences in cellular sensitivityto lysis, lytic peptide concentration can be manipulated to effect lysisof one cell type but not another at the same locus.

Synthetic lytic peptide analogs can also act as agents of eukaryoticcell proliferation. Peptides that promote lysis of transformed cellswill, at lower concentrations, promote cell proliferation in some celltypes. This stimulatory activity is thought to depend on thechannel-forming capability of the peptides, which somehow stimulatesnutrient uptake, calcium influx or metabolite release, therebystimulating cell proliferation (see Jaynes, J. M., Drug News &Perspectives 3: 69 1990!; and Reed, W. A. et al., Molecular Reproductionand Development 31: 106 1992!). Thus, at a given concentration, thesepeptides stimulate or create channels that can be beneficial to thenormal mammalian cell in a benign environment where it is not importantto exclude toxic compounds.

The synthetic lytic peptide analogs typically contain as few as 12 andas many as 40 amino acid residues. A phenylalanine residue is oftenpositioned at the amino terminus of the protein to provide an aromaticmoiety analogous to the tryptophan residue located near the aminoterminus of natural cecropins and a UV-absorbing moiety with which tomonitor the purification of the synthetic peptide. The basis for thedesign of these lytic peptide analogs is that a peptide of minimallength, having an amphipathic α-helical structural or a β-pleated sheetmotif, and overall positive charge density effects lytic activity.

Plant disease is one of the leading causes of crop loss in the world andis estimated to cause up to one third of total crop loss worldwide; forexample, in the potato losses associated with bacterial disease are ashigh as 25% of worldwide production. Additionally, the cultivation of afew species of plants in a concentrated area exacerbates the spread ofdisease. Recent advances in genetic engineering have lead to thedevelopment of plants with disease resistant phenotypes based on theexpression of recombinant DNA molecules. Transgenic tobacco plants wereengineered with both a wound inducible PiII promoter and a constitutive35S promoter to express two lytic peptides (SHIVA-1 and SB-37) withbacteriolytic activity. The SHIVA-1 plant demonstrated enhancedresistance to bacterial wilt caused by infection by Pseudomonassolanacearum (Jaynes, J. M., et al., Plant Science 89: 43 (1993);Destefano-Beltran, L., et al., Biotechnology in Plant Disease Control,pp. 175-189, Wiley-Liss (1993). Thus lytic peptides have valuable usesas anti-phytopathogenic agents. However, chemical synthesis of theselytic peptides is very expensive. Therefore, alternate, more economicaland efficient methods of synthesis are needed, such as in vivo synthesisin host cells using recombinant DNA methods.

Recombinant DNA molecules are produced by sub-cloning genes intoplasmids using a bacterial host intermediate. In principle thistechnique is straightforward. However, any sequence that interferes withbacterial growth through replication or production of products toxic tothe bacteria, such a lytic peptides, are difficult to clone. Often, hostbacterial cells containing mutated forms of the DNA sequences encodingtoxic products will be selected. These mutations can result in eitherdecreased expression or production of an inactive product. Bacteria willeven insert mutations that prevent expression of a potentially toxicproduct in cloned genes controlled by a eukaryotic promoter that is notactive in prokaryotes. The effect of this selection of mutated speciesleads to an Inability to isolate sub-clones containing a non-mutatedgene of choice. Thus, some sub-cloned genes are unstable in theirbacterial hosts, although this instability can only be shownempirically. The bacteriolytic activity of the lytic peptides is anobstacle to the production of stable recombinant DNA molecules thatexpress the genes at high levels.

For example, in an attempt to sub-clone into a standard plasmid vector agene coding for frog magainin, a natural lytic peptide, bacterialtransformants contained deletion mutations in the magainin codingregion. Another attempt was made to sub-clone a synthetic lytic peptide(SEQ ID NO. 98) into a standard plasmid vector (pUC19) containing theCauliflower Mosaic virus 35S promoter. The resulting transformants werescreened by polymerase chain reaction (PCR). However, out of 30colonies, only 2 sub-clones gave faint positive signals. These twosub-clones were sequenced. The sequence showed that one clone had apoint mutation that introduced a stop codon 3/4 of the way through thelytic peptide, and the other clone had a point mutation that changed thestart codon from methionine to isoleucine. Both mutations would preventthe biosynthesis of the protein. Four more clones were analyzed, and ofthese four, one was sub-cloned an the wrong orientation, and threeothers had mutations introduced into the sequence. One of thesesub-clones was selected for further analysis, but it inhibited thegrowth of its E. coli host. Thus, the production of recombinant DNAmolecules coding for lytic peptides is difficult due to the uncertaintyin obtaining the correct sub-clone.

Ubiquitin is a small, highly conserved protein present in alleukaryotes. Ubiquitins are encoded by gene families that arecharacterized by two types of basic structures. Polyubiquitin genescontain several direct repeats of ubiquitin, and ubiquitin-ribosomalfusion genes encode a single ubiquitin unit fused to the coding regionfor a small ribosomal associated protein. Both of these gene types aretranslated as polyproteins and then are processed By an endogenousubiquitin hydrolase present in eukaryotes to release multiple ubiquitinproteins or ubiquitin and the ribosomal associated protein. A number ofubiquitin cDNAs or genomic clones have been isolated, including plantubiquitin cDNAs and genomic clones from the potato (Garbarino, J. andBelknap, W., Plant Molecular Biology 24: 119 (1994); Garbarino. J. etal., Plant Molecular Biology 20: 235 (1992)).

U.S. Pat. Nos. 5,093,242 and 5,132,213 to Bachmair et al. teach the useof a ubiquitin cloning vector as a method of producing specified proteinamino-termini. A recombinant DNA molecule was constructed with a proteincoding gene fused at its amino terminus to a ubiquitin coding gene. Dueto translation as a polypeptide and cleavage by hydrolases, a proteinwith any amino acid at the amino terminus can be generated. The aminoterminus can be used to control the metabolic stability of the protein.However, the metabolic stability of the protein is dependent on theresulting amino acid at the amino-terminus, not the generation of atranslation polypeptide.

The forgoing facts suggest that although lytic peptides as a class mayinclude species that are efficacious in destroying bacteria, neoplasticcells, fungi, virus-infected cells, and protozoa, this lyticcharacteristic also decreases the stability of sub-cloned lytic peptidesin host cells. This decreased stability hinders efforts to develop amore economical and efficient means of synthesizing lytic peptides.

It would therefore be a significant advance in the art, and iscorrespondingly an object of the present invention to develop a methodof sub-cloning nucleotide sequences coding for lytic peptides intoexpression vectors, providing gene constructs with enhanced stabilityand gene expression and reduced toxicity.

SUMMARY OF THE INVENTION

The present invention relates generally to ubiquitin-lytic peptidefusion nucleic acid expression vectors comprising a promoter andubiquitin polypeptide coding sequence ligated to a lytic peptide,ubiquitin-lytic peptide fusion protein products, and methods of makingand using the same, as hereinafter more fully described.

It is another object of the invention to provide ubiquitin-lytic peptidefusion expression vectors and protein products derived therefrom.

It is another object of the invention to provide ubiquitin-lytic peptidefusion expression vectors that are expressed in plants having utilityfor promoting wound healing and combatting bacterial infections inplants.

It is a further object of this invention to provide ubiquitin-lyticpeptide fusion polypeptides having utility for combatting protozoalinfections, neoplasias, fungal infections, viral infections, andbacterial infections in mammals and plants.

It is yet another object of this invention to develop a method ofsub-cloning polypeptide sequences in ubiquitin-fusion expression vectorswith enhanced stability and gene expression.

It is yet another object of this invention to provide expression vectorscontaining constitutive and wound inducible ubiquitin promoters that areexpressed in eukaryotic cells.

It is yet another object of this invention to provide expression vectorswith procaryotic promoters that express ubiquitin-lytic peptide fusiongenes in procaryotic hosts, the products of which can be cleaved invitro by ubiquitin hydrolases.

These and other objects and advantages will be more fully apparent fromthe ensuing disclosure and claims.

BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1 is a map of a recombinant nucleic acid expression vectorpUCUbi3-LP98 containing a 920 bp ubiquitin-ribosomal fusion genepromoter region linked to a 228 bp coding region for a ubiquitinpolypeptide with a six bp BamHI site at the 3' end (SEQ ID NO. 93) thatis fused at its 3' end to a gene coding for a lytic peptide (D5D*, SEQID NO. 98). The Ubi3 ubiquitin-lytic peptide nucleotide sequencecorresponds to SEQ ID NO. 92. A nopaline synthase polyadenylation signalis located at the 3' end of the lytic peptide gene.

FIG. 2 is a map of a recombinant nucleic acid expression vectorpUCUbi7-LP98 containing a 1220 bp polyubiquitin promoter region and 568bp intron linked to a 228 bp coding region for a ubiquitin polypeptidewith a six bp BamHI site at the 3' end (SEQ ID NO. 96) that is fused atits 3' end to a gene coding for a lytic peptide (D5D*, SEQ ID NO. 98).The Ubi7 ubiquitin-lytic peptide nucleotide sequence corresponds to SEQID NO. 95. A nopaline synthase polyadenylation signal is located at the3' end of the lytic peptide gene.

DETAILED DESCRIPTION OF THE INVENTION AND PREFERRED EMBODIMENTS THEREOF

The disclosures of prior co-pending U.S. patent application No.08/039,620 filed Jun. 4, 1993 in the names of Jesse M. Jaynes and GordonR. Julian, U.S. patent application No. 08/148,889 filed Nov. 8, 1993 inthe name of Gordon R. Julian, U.S. patent application No. 08/148,491filed Nov. 8, 1993 in the name of Gordon R. Julian, U.S. patentapplication No. 08/225,476 filed Apr. 8, 1994 in the names of Jesse M.Jaynes and Gordon R.

Julian, and U.S. patent application No. 08/231,730 filed Apr. 20, 1994in the names of Jesse M. Jaynes and Gordon R. Julian, are all herebyincorporated herein by reference in their entirety.

The term "amphipathic" as used herein refers to the distribution ofhydrophobic and hydrophilic amino acid residues along opposing faces ofan α-helix structure or other secondary conformation, which results inone face of the α-helix structure being predominantly hydrophobic andthe other ace being predominantly hydrophilic. The degree of amphipathyof a peptide can be assessed by plotting the sequential amino acidresidues on an Edmunson helical wheel (see also Kamtekar, S. et al.,Science 262: 1680 (1993). The terms "peptide" and "polypeptide" as usedherein refer to a molecule composed of a chain of amino acid residuesand is intended to be construed as inclusive of polypeptides andpeptides per se having molecular weights of up to 10,000 daltons, aswell as proteins having molecular weights of greater that about 10,000daltons, wherein the molecular weights are number average molecularweights. The term is also intended to be construed as inclusive offunctional equivalents thereof when used in reference to a specificpeptide coding sequence in the specification and claims herein.Functional equivalents of peptides and polypeptides include but are notlimited to deletions, additions, and substitutions of amino acids in thepolypeptide or peptide chain that do not adversely affect the overallfunction of the resulting peptide or polypeptide.

The term "plasmid" as used herein refers to a DNA molecule that iscapable of autonomous replication within a host cell, eitherextrachromosomaily or as part of the host cell chromosome(s). Thestarting plasmids herein are commercially available, are publiclyavailable on an unrestricted basis, or can be constructed from suchavailable plasmids as disclosed herein and/or in accordance wishpublished procedures. In certain instances, as will be apparent to theordinarily skilled artisan, other plasmids known in the art may be usedinterchangeable with plasmids described herein.

The term "ligation" as used herein refers to the process of formingphosphodiester bonds between two double-stranded DNA fragments. Unlessotherwise specified, ligation is accomplished using standard proceduresknown to one skilled in the art.

The term "polymerase chain reaction," or "PCR" as used herein refers toa method for amplification of a desired nucleotide sequence in vitro, asdescribed in U.S. Pat. No. 4,683,195, herein incorporated by referencein its entirety.

The term "nucleic acid" as used herein refers to deoxyribonucleic acidmolecules (DNA) composed of a chain of deoxyribonucleotides andribonucleic acid molecules (RNA) composed of a chain of ribonucleotides.The term "nucleic acid" as used herein is to be construed as includingfunctional equivalents thereof when used in reference to a specificnucleotide sequence in the specification and claims herein. Functionalequivalents of nucleic acid molecules include synonymous codingsequences with one or more codon substitutions and deletions oradditions that do not effect the overall function of the resultingnucleic acid molecule. The degeneracy of the genetic code is well knownto the art; therefore, synonymous coding sequences with one or morecodon substitutions can be readily determined by one of ordinary skillin the art. Synonymous nucleotide coding sequences vary from theexemplified coding sequences but encode proteins of the same amino acidsequences as those specifically provided herein or proteins with similarfunction and are therefore also regarded as functional equivalentsthereof.

The term "promoter" as used herein refers to an untranslated (i.e. onethat does not result in a peptide or protein product) sequence upstreamof the polypeptide coding region of a nucleotide sequence that controlstranscription of a gene. Promoters typically fall into two classes,constitutive and inducible. Inducible promoters initiate high levels oftranscription of the nucleic acid under their control in response toexternal stimuli. Constitutive promoters maintain a relatively constantlevel of transcription in a given cell. Suitable promoters for use inthe present may include both procaryotic and eukaryotic promoters, withall ubiquitin promoters being preferred, solanaceous plant ubiquitinpromoters being highly preferred, and potato ubiquitin promoters beingmost preferred. Additional control sequences such as ribosomal bindingsites and enhancers may be included as control sequences when necessary.

The term "polyadenylation" sites as used herein refers to a controlsequence located on the 3' end of a gene construct that provides asignal for cleavage and polyadenylation of the transcription unitexpressed from the promoter. These control sequences are known to oneskilled in the art

The term "expression" as used herein refers to transcription and ortranslation of a nucleic acid sequence coding for a protein or peptide.

In one embodiment, the present invention is directed to an isolatednucleotide sequence comprising a gene coding for a ubiquitin polypeptideand functional equivalents thereof, linked to a ubiquitin promoter andfunctional equivalents thereof. Suitable ubiquitin promoters for use inthe present invention include, but are not limited to, ubiquitinpromoters from solanaceous plants. Preferably, the ubiquitin promoter isa potato plant ubiquitin promoter and most preferably it is the potatoUbi3 or Ubi7 promoter. In embodiments wherein the isolated nucleotidesequence codes for the potato Ubi3 promoter linked to a gene coding fora ubiquitin polypeptide it has a nucleotide sequence according to SEQ IDNO. 93. The Ubi3 promoter alone also has utility as constitutivepromoter in eukaryotes.

In embodiments wherein the isolated nucleotide sequence codes for thepotato Ubi7 promoter linked to a gene coding for a ubiquitin polypeptideit has a nucleotide sequence according to SEQ ID NO. 96. The Ubi7nucleotide sequence according to SEQ ID NO. 96 includes an intron thatis part of the ubiquitin transcription unit. The intron is not requiredfor gene expression from the Ubi7 promoter, thus the Ubi7 promoterregion without the intron can be considered as a specific functionalequivalent of the Ubi7 promoter. The Ubi7 promoter alone, with orwithout the intron, has utility as a wound inducible promoter ineukaryotes.

Preferably, the nucleotide sequence comprising the isolated ubiquitinpromoter and gene coding for a ubiquitin polypeptide further comprises agene coding for a lytic peptide ligated to the 3' end of the gene codingfor a ubiquitin polypeptide. Suitable genes coding for a lytic peptidehave a nucleotide sequence coding for any one of the amino acidsequences according to SEQ ID NO. 1-91 and 97-98.

In one preferred embodiment, the present invention is directed to anisolated nucleotide sequence comprising a gene coding for a lyticpeptide ligated to the 3' end of the gene coding for a ubiquitinpolypeptide linked to the Ubi3 ubiquitin promoter having a nucleotidesequence according to SEQ ID NO. 92. In an alternative of thisembodiment, the present invention is directed to an isolated nucleotidesequence comprising a gene coding for a lytic peptide ligated to the 3'end of the gene coding for a ubiquitin polypeptide linked to a Ubi7ubiquitin promoter having a nucleotide sequence according to SEQ ID NO.95.

In another embodiment, the present invention is directed to arecombinant nucleic acid expression vector. The vector is characterizedin that it comprises a nucleotide sequence wherein a gene coding for aubiquitin polypeptide is linked to a ubiquitin promoter. Preferably, thepresent invention is directed to a recombinant nucleic acid expressionvector characterized in that it further comprises a nucleotide sequencewherein a gene coding for a lytic peptide is ligated to the 3' end ofthe gene coding for a ubiquitin polypeptide linked to a ubiquitinpromoter. Suitable vectors for use in this invention include anyeukaryotic or procaryotic expression vectors known in the art.Preferable vectors for use in this invention are pUC19 and pCGN1547.

In another embodiment, the present invention is directed to a host cellthat is transformed by a recombinant DNA expression vector comprising agene coding for a ubiquitin polypeptide linked to a ubiquitin promoter.Suitable host cells for transformation in the present invention includeall known bacterial host cells, with all strains of Escherichia coli andAgrobacterium tumefaciens being preferred. Preferably, the presentinvention is directed to a host cell the recombinant DNA expressionvector further comprises a gene coding for a lytic peptide ligated tothe 3' end of the gene coding for a ubiquitin polypeptide linked to aubiquitin promoter. Suitable genes coding for a lytic peptide have anucleotide sequence coding for any one of the amino acid sequencesaccording :to SEQ ID NO. 1-91 and 97-98.

Preferably, the present invention is directed to a solanaceous planthost cell that is transformed by a recombinant DNA expression vector.Most preferably the solanaceous plant cell is a potato plant host cell.

In another embodiment, the present invention is directed to an isolatednucleotide sequence and functional equivalents thereof coding for alytic peptide, where the nucleotide sequence has a sequence coding forany one of the amino acid sequences according to SEQ ID NO. 1-91 and97-98.

In yet another embodiment, the present invention is directed to apurified ubiquitin polypeptide and functional equivalents thereof havingan amino acid sequence according to SEQ ID NO. 94. This embodiment canfurther comprise a lytic peptide translationally fused to the carboxyterminus of a ubiquitin polypeptide.

In another embodiment, the present invention is directed to a method ofsub-cloning nucleotide sequences coding for lytic peptides andexpressing such sequences in cells. The method comprises a first stepwherein a recombinant nucleic acid containing a gene coding for a lyticpeptide ligated to a gene coding for a ubiquitin polypeptide linked to aubiquitin promoter is produced in a first host cell. Suitable first hostcells include any known bacterial host cells. Preferably, the first hostcell is either an Escherichia coli cell or an Agrobacterium tumefacienscell.

If the peptides are sub-cloned using such a ubiquitin-fusion expressionvector, the following advantage results: the lytic peptide geneconstructs have increased stability in the bacterial host. While notwishing to be bound by any one theory, the present inventors believethat the stability is due to the ubiquitin protein coding nucleic acidregion fused to the 5' end of the lytic peptide nucleic acid sequence.Bacteria do not contain the endogenous hydrolase necessary for cleavageof the ubiquitin fusion protein, so the gene constructs are not toxic tobacteria, since active lytic peptide cannot released. Thus functionalequivalents of the ubiquitin fusion polypeptide include any ubiquitinmolecule that is capable of deceiving the host cell into viewing thegene construct and its products as non-toxic.

In a variation of this embodiment, the recombinant nucleic acid vectoris isolated from the first host cell and expressed in a second hostcell. Suitable second host cells are plant and animal cells, preferablya solanaceous plant cell, and most preferably a potato plant cell. Inthe second host cell the fusion gene is expressed at high levels and thepolyprotein is cleaved by endogenous ubiquitin hydrolases to produceactive lytic peptide. These transgenic hosts provide from the expressionvector lytic peptides in vivo to combat bacterial infections, fungalinfections, protozoal infections, virus infections, and neoplasias. Inaddition, expression vectors containing ubiquitin promoters that areeither constitutive or wound inducible are used to express peptides ineukaryotes.

The present invention is also directed to a method of sub-cloningnucleotide sequences coding for lytic peptides and expressing suchsequences in cells. The method comprises producing in a host cell arecombinant nucleic acid expression vector comprising a gene coding fora lytic peptide ligated to the 3' end of a gene coding for a ubiquitinpromoter linked to a procaryotic promoter sequence. Suitable procaryoticpromoters include those known to one skilled in the art to be active inprokaryotes and used in plasmid vectors for bacterial gene expression.

The recombinant nucleic acid expression vector is expressed in the hostcell and ubiquitin-lytic peptide fusion polypeptides are isolated fromthe host. Preferably, the host cell is either an Escherichia coli cellor an Agrobacterium tumefaciens cell. The isolated ubiquitin-lyticpeptide fusion polypeptides are then cleaved in vitro by ubiquitinhydrolases to release the lytic peptides from the ubiquitin polypeptide(see U.S. Pat. No. 5,196,321 to Bachmair et al.). The active lyticpeptides are then used to treat bacterial infections, fungal infections,protozoal infections, virus infections, and neoplasias. These isolatedlytic peptides are in some instances glyoxylated or methylated in vitroto stabilize against proteolytic digestion in vivo.

Ubiquitin fusion expression vectors thus have broad utility as cloningand expression vectors to stabilize and sub-clone lytic peptidesnucleotide sequences, as well as a wide variety of protein codingnucleic acid sequences that are otherwise toxic to their hosts. Theubiquitin-lytic peptide expression vectors also have broad utility as aneconomical and efficient means to synthesize lytic peptides in hostcells. These lytic peptides have utility for combatting protozoalinfections, neoplasias, fungal infections, viral infections, andbacterial infections in mammals and plants.

The features and advantages of the invention are more fully shown by thefollowing illustrative examples and embodiments, which are not to belimitingly construed as regard the broad scope, utility, andapplicability of the invention.

EXAMPLE 1 Representative Lytic Peptides and Ubiquitin Polypeptide

Set out in Table 1 below as illustrative examples of lytic peptides arethe amino acid sequences of families of related lytic peptides. Theselytic peptides are designated for ease of reference as SEQ ID NO. 1-91and 97-98. Nucleic acid sequences coding for these lytic peptides andfunctional equivalents thereof represent examples of lytic peptidenucleic acid sequences that are sub-cloned to make ubiquitin-lyticpeptide fusion gene constructs and polypeptides. The ubiquitinpolypeptide, designated for ease of reference as SEQ ID NO. 94, andfunctional equivalents thereof, represents an example of the 5' fusionubiquitin polypeptide.

                                      TABLE 1    __________________________________________________________________________    LYTIC PEPTIDE SEQUENCES    __________________________________________________________________________    SEQ ID NO. 1    Phe Ala Val Ala Val Lys Ala Val Lys Lys Ala Val Lys Lys Val Lys     1               5                  10                  15    Lys Ala Val Lys Lys Ala Val Lys Lys Lys Lys                20                   25    SEQ ID NO. 2    Phe Ala Val Ala Val Lys Ala Val Ala Val Lys Ala Val Lys Lys Ala     1               5                  10                  15    Val Lys Lys Val Lys Lys Ala Val Lys Lys Ala Val Lys Lys Lys Lys                 20                  25                  30    SEQ ID NO. 3    Phe Ala Val Ala Val Lys Ala Val Ala Val Lys Ala Val Ala Val Lys     1               5                  10                  15    Ala Val Lys Lys Ala Val Lys Lys Val Lys Lys Ala Val Lys Lys Ala                20                   25                 30    Val Lys Lys Lys Lys            35    SEQ ID NO. 4    Phe Ala Val Ala Val Lys Ala Val Lys Lys Ala Val Lys Lys Val Lys     1               5                  10                  15    Lys Ala Val Lys Lys Ala Val                20    SEQ ID NO. 5    Phe Ala Val Ala Val Lys Ala Val Ala Val Lys Ala Val Lys Lys Ala     1               5                  10                  15    Val Lys Lys Val Lys Lys Ala Val Lys Lys Ala Val                20                  25    SEQ ID NO. 6    Phe Ala Val Ala Val Lys Ala Val Ala Val Lys Ala Val Ala Val Lys     1               5                  10                  15    Ala Val Lys Lys Ala Val Lys Lys Val Lys Lys Ala Val Lys Lys Ala                20                   25                 30    Val    SEQ ID NO. 7    Phe Ala Val Gly Leu Arg Ala Ile Lys Arg Ala Leu Lys Lys Leu Arg     1               5                  10                  15    Arg Gly Val Arg Lys Val Ala Lys Arg Lys Arg                20                  25    SEQ ID NO. 8    Phe Ala Val Gly Leu Arg Ala Ile Lys Arg Ala Leu Lys Lys Leu Arg     1               5                  10                  15    Arg Gly Val Arg Lys Val Ala                20    SEQ ID NO. 9    Lys Arg Lys Arg Ala Val Lys Arg Val Gly Arg Arg Leu Lys Lys Leu     1               5                  10                  15    Ala Arg Lys Ile Ala Arg Leu Gly Val Ala Phe                20                   25    SEQ ID NO. 10    Ala Val Lys Arg Val Gly Arg Arg Leu Lys Lys Leu Ala Arg Lys Ile     1               5                  10                  15    Ala Arg Leu Gly Val Ala Phe                20    SEQ ID NO. 11    Phe Ala Val Gly Leu Arg Ala Ile Lys Arg Ala Leu Lys Lys Leu Arg     1               5                  10                  15    Arg Gly Val Arg Lys Val Ala Lys Arg Lys Arg Lys Lys Asp Leu                20                   25                 30    SEQ ID NO. 12    Phe Ala Val Gly Leu Arg Ala Ile Lys Arg Ala Leu Lys Lys Leu Arg     1               5                  10                  15    Arg Gly Val Arg Lys Val Ala Lys Asp Leu                20                   25    SEQ ID NO. 13    Lys Arg Lys Arg Ala Val Lys Arg Val Gly Arg Arg Leu Lys Lys Leu     1               5                  10                  15    Ala Arg Lys Ile Ala Arg Leu Gly Val Ala Phe Lys Asp Leu                20                  25                  30    SEQ ID NO. 14    Ala Val Lys Arg Val Gly Arg Arg Leu Lys Lys Leu Ala Arg Lys Ile     1               5                  10                  15    Ala Arg Leu Gly Val Ala Phe Lys Asp Leu                20                  25    SEQ ID NO. 15    Lys Lys Lys Lys Phe Val Lys Lys Val Ala Lys Lys Val Lys Lys Val     1               5                  10                  15    Ala Lys Lys Val Ala Lys Val Ala Val Ala Val                20                  25    SEQ ID NO. 16    Lys Lys Lys Lys Phe Val Lys Lys Val Ala Lys Lys Val Lys Lys Val     1               5                  10                  15    Ala Lys Lys Val Ala Lys Val Ala Val Ala Lys Val Ala Val Ala Val                20                   25                 30    SEQ ID NO. 17    Lys Lys Lys Lys Phe Val Lys Lys Val Ala Lys Lys Val Lys Lys Val     1               5                  10                  15    Ala Lys Lys Val Ala Lys Val Ala Val Ala Lys Val Ala Val Ala Lys                20                   25                 30    Val Ala Val Ala Val            35    SEQ ID NO. 18    Phe Val Lys Lys Val Ala Lys Lys Val Lys Lys Val Ala Lys Lys Val     1               5                  10                  15    Ala Lys Val Ala Val Ala Val                20    SEQ ID NO. 19    Phe Val Lys Lys Val Ala Lys Lys Val Lys Lys Val Ala Lys Lys Val     1               5                  10                  15    Ala Lys Val Ala Val Ala Lys Val Ala Val Ala Val                20                  25    SEQ ID NO. 20    Phe Val Lys Lys Val Ala Lys Lys Val Lys Lys Val Ala Lys Lys Val     1               5                  10                  15    Ala Lys Val Ala Val Ala Lys Val Ala Val Ala Lys Val Ala Val Ala                20                  25                  30    Val    SEQ ID NO. 21    Lys Lys Lys Lys Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val     1               5                  10                  15    Ala Lys Val Ala Lys Lys Val Ala Lys Lys Val                20                  25    SEQ ID NO. 22    Lys Lys Lys Lys Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val     1               5                  10                  15    Ala Lys Val Ala Lys Lys Val Ala Lys Lys Val Ala Lys Lys Val Ala                20                  25                  30    SEQ ID NO. 23    Lys Lys Lys Lys Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val     1               5                  10                  15    Ala Lys Val Ala Lys Lys Val Ala Lys Lys Val Ala Lys Lys Val Ala                20                  25                  30    Lys Val Ala Lys Lys            35    SEQ ID NO. 24    Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val Ala Lys Val Ala     1               5                  10                  15    Lys Lys Val Ala Lys Lys Val                20    SEQ ID NO. 25    Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val Ala Lys Val Ala     1               5                  10                  15    Lys Lys Val Ala Lys Lys Val Ala Lys Lys Val Ala                20                  25    SEQ ID NO. 26    Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val Ala Lys Val Ala     1               5                  10                  15    Lys Lys Val Ala Lys Lys Val Ala Lys Lys Val Ala Lys Val Ala Lys                20                  25                  30    Lys    SEQ ID NO. 27    Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val Ala Lys Val Ala     1               5                  10                  15    Lys Lys Val Ala Lys Lys Val Lys Lys Lys Lys                20                  25    SEQ ID NO. 28    Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val Ala Lys Val Ala     1               5                  10                  15    Lys Lys Val Ala Lys Lys Val Ala Lys Lys Val Ala Lys Lys Lys Lys                20                  25                  30    SEQ ID NO. 29    Phe Val Lys Lys Val Ala Lys Val Ala Lys Lys Val Ala Lys Val Ala     1               5                  10                  15    Lys Lys Val Ala Lys Lys Val Ala Lys Lys Val Ala Lys Val Ala Lys                20                  25                  30    Lys Lys Lys Lys Lys            35    SEQ ID NO. 30    Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys Lys Lys Lys Lys     1               5                  10                  15    SEQ ID NO. 31    Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys     1               5                  10                  15    Ala Lys Lys Lys Lys                20    SEQ ID NO. 32    Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys     1               5                  10                  15    Ala Lys Val Lys Ala Lys Val Lys Lys Lys Lys                20                  25    SEQ ID NO. 33    Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys     1               5                  10    SEQ ID NO. 34    Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys     1               5                  10                  15    Ala    SEQ ID NO. 35    Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys     1               5                  10                  15    Ala Lys Val Lys Ala Lys Val                20    SEQ ID NO. 36    Lys Lys Lys Lys Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys     1               5                  10                  15    SEQ ID NO. 37    Lys Lys Lys Lys Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys     1               5                  10                  15    Ala Lys Val Lys Ala                20    SEQ ID NO. 38    Lys Lys Lys Lys Phe Lys Val Lys Ala Lys Val Lys Ala Lys Val Lys     1               5                  10                  15    Ala Lys Val Lys Ala Lys Val Lys Ala Lys Val                20                  25    SEQ ID NO. 39    Phe Lys Lys Val Lys Lys Val Ala Lys Lys Val Cys Lys Cys Val Lys     1               5                  10                  15    Lys Ala Val Lys Lys Val`Lys Lys Phe                20                  25    SEQ ID NO. 40    Phe Ala Val Ala Val Lys Ala Val Lys Lys Ala Val Lys Lys Val Lys     1               5                  10                  15    Lys Ala Val Lys Lys Ala Val Cys Cys Cys Cys                20                  25    SEQ ID NO. 41    Cys Cys Cys Cys Phe Val Lys Lys Val Ala Lys Lys Val Lys Lys Val     1               5                  10                  15    Ala Lys Lys Val Ala Lys Val Ala Val Ala Val                20                  25    SEQ ID NO. 42    Phe Ala Val Ala Val Lys Ala Val Lys Lys Ala Val Lys Lys Val Lys     1               5                  10                  15    Lys Ala Val Lys Lys Ala Val Ser Ser Ser Ser                20                  25    SEQ ID NO. 43    Ser Ser Ser Ser Phe Val Lys Lys Val Ala Lys Lys Val Lys Lys Val     1               5                  10                  15    Ala Lys Lys Val Ala Lys Val Ala Val Ala Val                20                  25    SEQ ID NO. 44    Phe Ala Leu Ala Leu Lys Ala Leu Lys Lys Ala Leu Lys Lys Leu Lys     1               5                  10                  15    Lys Ala Leu Lys Lys Ala Leu                20    SEQ ID NO. 45    Leu Ala Lys Lys Leu Ala Lys Lys Leu Lys Lys Leu Ala Lys Lys Leu     1               5                  10                  15    Ala Lys Leu Ala Leu Ala Phe                20    SEQ ID NO. 46    Phe Ala Phe Ala Phe Lys Ala Phe Lys Lys Ala Phe Lys Lys Phe Lys     1               5                  10                  15    Lys Ala Phe Lys Lys Ala Phe                20    SEQ ID NO. 47    Phe Ala Ile Ala Ile Lys Ala Ile Lys Lys Ala Ile Lys Lys Ile Lys     1               5                  10                  15    Lys Ala Ile Lys Lys Ala Ile                20    SEQ ID NO. 48    Phe Ala Lys Lys Phe Ala Lys Lys Phe Lys Lys Phe Ala Lys Lys Phe     1               5                  10                  15    Ala Lys Phe Ala Phe Ala Phe                20    SEQ ID NO. 49    Phe Lys Arg Leu Ala Lys Ile Lys Val Leu Arg Leu Ala Lys Ile Lys     1               5                  10                  15    Arg    SEQ ID NO. 50    Lys Leu Lys Leu Ala Val Lys Leu Val Gly Leu Leu Arg Lys Lys Arg     1               5                  10                  15    Ala Leu Lys Ile Ala Leu Arg Gly Val Ala Lys Arg Ala Gly Arg Leu                20                  25                  30    Ala Val Arg Lys Phe            35    SEQ ID NO. 51    Phe Ala Arg Ala Arg Lys Ala Arg Lys Lys Ala Arg Lys Lys Arg Lys     1               5                  10                  15    Lys Ala Arg Lys Lys Ala Arg Lys Asp Arg                20                  25    SEQ ID NO. 52    Phe Ala Val Ala Val Cys Ala Val Cys Cys Ala Val Cys Cys Val Cys     1               5                  10                  15    Cys Ala Val Cys Cys Ala Val                20    SEQ ID NO. 53    Phe Ala Val Ala Val Ser Ala Val Ser Ser Ala Val Ser Ser Val Ser     1               5                  10                  15    Ser Ala Val Ser Ser Ala Val                20    SEQ ID NO. 54    Phe Ala Val Ala Val Ser Ala Val Ser Ser Ala Val Ser Ser Val Ser     1               5                  10                  15    Ser Ala Val Ser Ser Ala Val Ser Ser Ser Ser                20                  25    SEQ ID NO. 55    Phe Ala Lys Lys Phe Ala Lys Lys Phe Lys Lys Phe Ala Lys Lys Phe     1               5                  10                  15    Ala Lys Phe Ala Phe Ala Phe Lys Lys Lys Lys                20                  25    SEQ ID NO. 56    Lys Lys Lys Lys Phe Ala Lys Lys Phe Ala Lys Lys Phe Lys Lys Phe     1               5                  10                  15    Ala Lys Lys Phe Ala Lys Phe Ala Phe Ala Phe                20                  25    SEQ ID NO. 57    Phe Ala Arg Lys Phe Leu Lys Arg Phe Lys Lys Phe Val Arg Lys Phe     1               5                  10                  15    Ile Arg Phe Ala Phe Leu Phe                20    SEQ ID NO. 58    Phe Ala Arg Lys Phe Leu Lys Arg Phe Lys Lys Phe Val Arg Lys Phe     1               5                  10                  15    Ile Arg Phe Ala Phe Leu Phe Lys Arg Lys Arg                20                  25    SEQ ID NO. 59    Lys Arg Lys Arg Phe Ala Arg Lys Phe Leu Lys Arg Phe Lys Lys Phe     1               5                  10                  15    Val Arg Lys Phe Ile Arg Phe Ala Phe Leu Phe                20                  25    SEQ ID NO. 60    Ile Ala Lys Lys Ile Ala Lys Lys Ile Lys Lys Ile Ala Lys Lys Ile     1               5                  10                  15    Ala Lys Ile Ala Ile Ala Ile                20    SEQ ID NO. 61    Ile Ala Lys Lys Ile Ala Lys Lys Ile Lys Lys Ile Ala Lys Lys Ile     1               5                  10                  15    Ala Lys Ile Ala Ile Ala Ile Lys Lys Lys Lys                20                  25    SEQ ID NO. 62    Lys Lys Lys Lys Ile Ala Lys Lys Ile Ala Lys Lys Ile Lys Lys Ile     1               5                  10                  15    Ala Lys Lys Ile Ala Lys Ile Ala Ile Ala Ile                20                  25    SEQ ID NO. 63    Ile Ala Arg Lys Ile Leu Lys Arg Ile Lys Lys Ile Val Arg Lys Phe     1               5                  10                  15    Ile Arg Ile Ala Ile Leu Ile                20    SEQ ID NO. 64    Ile Ala Arg Lys Ile Leu Lys Arg Ile Lys Lys Ile Val Arg Lys Phe     1               5                  10                  15    Ile Arg Ile Ala Ile Leu Ile Lys Arg Lys Arg                20                  25    SEQ ID NO. 65    Lys Arg Lys Arg Ile Ala Arg Lys Ile Leu Lys Arg Ile Lys Lys Ile     1               5                  10                  15    Val Arg Lys Phe Ile Arg Ile Ala Ile Leu Ile                20                  25    SEQ ID NO. 66    Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg Ala Lys Ile Lys     1               5                  10                  15    Leu    SEQ ID NO. 67    Lys Arg Lys Arg Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg     1               5                  10                  15    Ala Lys Ile Lys Leu                20    SEQ ID NO. 68    Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg Ala Lys Ile Lys     1               5                  10                  15    Leu Lys Arg Lys Arg                20    SEQ ID NO. 69    Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg Ala Lys Ile Lys     1               5                  10                  15    Leu Arg Val Lys Leu Lys Ile                20    SEQ ID NO. 70    Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg Ala Lys Ile Lys     1               5                  10                  15    Leu Arg Val Lys Leu Lys Ile Lys Arg Lys Arg                20                  25    SEQ ID NO. 71    Lys Arg Lys Arg Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg     1               5                  10                  15    Ala Lys Ile Lys Leu Arg Val Lys Leu Lys Ile                20                  25    SEQ ID NO. 72    Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg Ala Lys Ile Lys     1               5                  10                  15    Leu Arg Val Lys Leu Lys Ile Arg Ala Arg Ile Lys Leu                20                  25    SEQ ID NO. 73    Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg Ala Lys Ile Lys     1               5                  10                  15    Leu Arg Val Lys Leu Lys Ile Arg Ala Arg Ile Lys Leu Lys Arg Lys                20                  25                  30    Arg    SEQ ID NO. 74    Lys Arg Lys Arg Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg     1               5                  10                  15    Ala Lys Ile Lys Leu Arg Val Lys Leu Lys Ile Arg Ala Arg Ile Lys                20                  25                  30    Leu    SEQ ID NO. 75    Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg Ala Lys Ile Lys     1               5                  10                  15    Leu Val Phe Ala Ile Leu Leu                20    SEQ ID NO. 76    Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg Ala Lys Ile Lys     1               5                  10                  15    Leu Val Phe Ala Ile Leu Leu Lys Arg Lys Arg                20                  25    SEQ ID NO. 77    Lys Arg Lys Arg Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Leu Arg     1               5                  10                  15    Ala Lys Ile Lys Leu Val Phe Ala Ile Leu Leu                20                  25    SEQ ID NO. 78    Val Phe Ala Ile Leu Leu Phe Lys Leu Arg Ala Lys Ile Lys Val Arg     1               5                  10                  15    Leu Arg Ala Lys Ile Lys Leu                20    SEQ ID NO. 79    Val Phe Ala Ile Leu Leu Phe Lys Leu Arg Ala Lys Ile Lys Val Arg     1               5                  10                  15    Leu Arg Ala Lys Ile Lys Leu Arg Lys Arg                20                  25    SEQ ID NO. 80    Lys Arg Lys Arg Val Phe Ala Ile Leu Leu Phe Lys Leu Arg Ala Lys     1               5                  10                  15    Ile Lys Val Arg Leu Arg Ala Lys Ile Lys Leu                20                  25    SEQ ID NO. 81    Val Gly Glu Cys Val Arg Gly Arg Cys Pro Ser Gly Met Cys Cys Ser     1               5                  10                  15    Gln Phe Gly Tyr Cys Gly Lys Gly Pro Lys Tyr Cys Gly                20                  25    SEQ ID NO. 82    Val Gly Glu Cys Val Arg Gly Arg Cys Pro Ser Gly Met Cys Cys Ser     1               5                  10                  15    Gln Phe Gly Tyr Cys Gly Lys Gly Pro Lys Tyr Cys Gly Arg                20                  25                  30    SEQ ID NO. 83    Leu Gly Asp Cys Leu Lys Gly Lys Cys Pro Ser Gly Met Cys Cys Ser     1               5                  10                  15    Asn Tyr Gly Phe Cys Gly Arg Gly Pro Arg Phe Cys Gly Lys                20                  25                  30    SEQ ID NO. 84    Gln Cys Ile Gly Asn Gly Gly Arg Cys Asn Glu Asn Val Gly Pro Pro     1               5                  10                  15    Tyr Cys Cys Ser Gly Phe Cys Leu Arg Gln Pro Gly Gln Gly Tyr Gly                20                  25                  30    Tyr Cys Lys Asn Arg            35    SEQ ID NO. 85    Cys Ile Gly Asn Gly Gly Arg Cys Asn Glu Asn Val Gly Pro Pro Tyr     1               5                  10                  15    Cys Cys Ser Gly Phe Cys Leu Arg Gln Pro Asn Gln Gly Tyr Gly Val                20                  25                  30    Cys Arg Asn Arg            35    SEQ ID NO. 86    Cys Ile Gly Gln Gly Gly Lys Cys Gln Asp Gln Leu Gly Pro Pro Phe     1               5                  10                  15    Cys Cys Ser Gly Tyr Cys Val Lys Asn Pro Gln Asn Gly Phe Gly Leu                20                  25                  30    Cys Lys Gln Lys            35    SEQ ID NO. 87    Gln Lys Leu Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly     1               5                  10                  15    Asn Asn Asn Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg                20                  25                  30    His Gly Ser Cys Asn Tyr Val Phe Pro Ala His Lys            35                  40    SEQ ID NO. 88    Gln Arg Val Cys Asp Lys Pro Ser Gly Thr Trp Ser Gly Leu Cys Gly     1               5                  10                  15    Asn Asn Asn Ala Cys Arg Gln Asn Cys Ile Gln Val Asp Arg Ala Lys                20                  25                  30    Lys Gly Ser Cys Gln Phe Leu Tyr Pro Ala Lys Lys            35                  40    SEQ ID NO. 89    Gln Lys Leu Cys Gln Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly     1               5                  10                  15    Asn Asn Asn Ala Cys Lys Asn Gln Cys Ile Arg Leu Glu Lys Ala Arg                20                  25                  30    His Gly Ser Cys            35    SEQ ID NO. 90    Gln Arg Val Cys Asn Lys Pro Ser Gly Thr Trp Ser Gly Leu Cys Gly     1               5                  10                  15    Asn Asn Asn Ala Cys Arg Gln Asn Cys Ile Lys Val Asp Arg Ala Lys                20                  25                  30    Lys Gly Ser Cys            35    SEQ ID NO. 91    Met Leu Glu Glu Leu Phe Glu Glu Met Thr Glu Phe Ile Glu Glu Val     1               5                  10                  15    Ile Glu Thr Met                20    SEQ ID NO. 94    Met Gln Ile Phe Val Lys Thr Leu     1                5    Thr Gly Lys Thr Ile Thr Leu Glu Val Glu Ser Ser Asp Thr        10                  15                  20    Ile Asp Asn Val Lys Ala Lys Ile Gln Asp Lys Glu Gly Ile            25                  30                  35    Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gly Lys Gln Leu                40                   45                  50    Glu Asp Gly Arg Thr Leu Ala Asp Tyr Asn Ile Gln Lys Glu                    55                  60    Ser Thr Leu His Leu Val Leu Arg Leu Arg Gly Gly Gly Ser    65                  70                  75    SEQ ID NO. 97    Lys Arg Lys Arg Ala Val Lys Arg Val Gly Arg Arg Leu Lys Lys Leu     1               5                  10                  15    Ala Arg Lys Ile Ala Arg Leu Gly Val Ala Lys Leu Ala Gly Leu Arg                20                  25                  30    Ala Val Leu Lys Phe            35    SEQ ID NO. 98    Ala Val Lys Arg Val Gly Arg Arg Leu Lys Lys Leu Asp Arg Lys Ile     1               5                  10                  15    Asp Arg Leu Gly Val Asp Phe                20    __________________________________________________________________________

EXAMPLE 2 Construction of Ubiquitin-Lytic Peptide Fusion Plasmids WithUbiquitin-ribosomal Fusion Gene Promoter (Ubi3)

Exemplary and preferred pUC19 and pCGN1547 plasmid vectors containing apotato (Solanum tuberosum) ubiquitin-ribosomal fusion promoter (Ubi3), aregion coding for a ubiquitin polypeptide, and a gene coding for a lyticpeptide are constructed.

To obtain the genomic clone containing a ubiquitin-ribosomal fusionpromoter and ubiquitin polypeptide coding region, a αFIXII potatogenomic library is first prescreened using PCR. The PCR primers arehomologous to regions of the ubiquitin-ribosomal fusion cDNA (seeGarbarino J., et al., Plant Molecular Biology 20: 235(1992); GarbarinoJ. and Belknap W., Plant Molecular Biology 30 24: 119 (1994); both ofwhich are hereby incorporated by reference herein in their entirety). Aprimer 5' to the beginning ATG of ubiquitin and a primer complementaryto a sequence near the 5' end of the ribosomal protein are used.

The library is plated in 22 aliquots containing approximately 0.5×10⁶pfu (plaque forming units) each on an E. coli lawn. A plug is taken fromeach of the 22 resulting plaques and the eluant from each is subjectedto PCR under standard conditions. The PCR products are run on agarosegels. The gels are then blotted and probed with the ubiquitin codingregion of the ubiquitin-ribosomal fusion cDNA according to standardconditions. Two of the plugs produce PCR products that hybridize to thecDNA probe., Both of these are the correct size for the predictedubiquitin-ribosomal fusion genomic fragment.

The eluants from these two plugs are then plated and screened with theubiquitin coding region of the ubiquitin-ribosomal fusion cDNA accordingto standard conditions. For verification, the positive plaques from theinitial screen are replated and screened with a probe containing boththe ribosomal protein-coding region and the 3' end of the potatoubiquitin-ribosomal fusion cDNA.

The genomic clones are sequenced using Sequenase version 2.0 15 (UnitedStates Biochemical Corporation) or Promega fmol DNA Sequencing Systemusing standard conditions. A genomic clone containing both theubiquitin-ribosomal fusion promoter region and the ubiquitin-ribosomalfusion coding region is identified.

A chimeric gene is then constructed with a portion of the potatoubiquitin-ribosomal fusion genomic clone ligated to a lytic peptidegene. PCR is used to generate the Ubi3 promoter and ubiquitin portion ofthe chimeric gene. The Ubi3 promoter region includes the 920 bp promoterregion upstream of the ubiquitin ATG, and the ubiquitin polypeptidecoding region is 228 bp plus 6 bp of a BamHI restriction site at the 3'end (SEQ ID NO. 93). The primers contain BamHI restriction sites and arehomologous to the 5' end of the Ubi3 promoter and to the 3' end of theubiquitin polypeptide coding region. The ubiquitin-ribosomal fusiongenomic clone is used as the amplification template. This insert isfirst sub-cloned into she plasmid pCGN1547, as described in Garbarino etal., Plant Molecular Biology 24: 119 (1994). The Ubi3 insert is thenisolated from pCGN1547 using the BamHI sites and ligated into pUCl9under standard conditions. Transformation of E. coli is done accordingto standard conditions and correct sub-clones are confirmed by mini-prepor PCR DNA analysis. This plasmid is designated pUCUbi3.

A nucleotide fragment coding for the lytic peptide (corresponding to theamino acid sequence SEQ ID NO. 98) is synthesized using a nucleic acidsynthesizer, adding a stop codon to the 3' end, and used as a PCRtemplate. The 5' PCR primer homologous to the lytic peptide nucleotidesequence contains a BamHI site, and the 3' primer contains an XbaI site.These sites are used to sub-clone the PCR generated insert into pUC19. Anopaline synthase polyadenylation signal (NOS3' ) is then cloned 3' tothe lytic peptide sequence. Following sequence analysis, the BamHIinsert containing the Ubi3 promoter and ubiquitin coding region (SEQ IDNO. 93) is cloned 5' to the lytic peptide.

After transforming E. coli under standard conditions, pUC19 sub-clonesare selected for mini-prep or PCR DNA analysis according to standardconditions. The direction of the promoter is confirmed and the junctionsequences are verified by sequencing according to standard conditions.The resulting Ubi3 ubiquitin-lytic peptide fusion gene constructcorresponds to SEQ ID NO. 92. Unlike previous cloning attempts using theCaMV35S promoter, as described in the Background section, the sequencedoes not reveal any point mutations in the lytic peptide sub-clones. Theplasmid is stable in the E. coli host and did not inhibit its growth.

The resulting pUC19 recombinant plasmid is shown in the plasmid map inFIG. 1. The sequence for the Ubi3-ubiquitin insert containing theubiquitin-ribosomal fusion gene promoter and the ubiquitin coding regioncorresponds to SEQ ID NO. 93 in Table 2 below. The sequence for thechimeric Ubi3 ubiquitin-lytic peptide fusion gene construct correspondsto SEQ ID NO. 92 in Table 2 below. This plasmid is designated aspUCUbi3-LP98.

The entire Ubi3 ubiquitin-lytic peptide fusion gene construct, includingthe polyadenylation site, was isolated from pUC19 as an Asp718/HindIIIrestriction fragment and sub-cloned into the pCGN1547 Agrobacteriumvector for use in plant transformation (see McBride, et al., PlantMolecular Biology 14:269 (1990). This plasmid is designated aspCGNUbi3-LP98.

                                      TABLE 2    __________________________________________________________________________    NUCLEOTIDE SEQUENCE OF POTATO UBIQUITIN-RIBOSOMAL    FUSION PROMOTER (UBI3) AND UBIQUITIN CODING REGION    INSERT, AND UBIQUITIN-LYTIC PEPTIDE FUSION GENE CONSTRUCT    __________________________________________________________________________    SEQ ID NO. 92    CCAAAGCACA TACTTATCGA TTTAAATTTC ATCGAAGAGA TTAATATCGA                                        50    ATAATCATAT ACATACTTTA AATACATAAC AAATTTTAAA TACATATATC                                        100    TGGTATATAA TTAATTTTTT AAAGTCATGA AGTATGTATC AAATACACAT                                        150    ATGGAAAAAA TTAACTATTC ATAATTTAAA AAATAGAAAA GATACATCTA                                        200    GTGAAATTAG GTGCATGTAT CAAATACATT AGGAAAAGGG CATATATCTT                                        250    GATCTAGATA ATTAACGATT TTGATTTATG TATAATTTCC AAATGAAGGT                                        300    TTATATCTAC TTCAGAAATA ACAATATACT TTTATCAGAA CATTCAACAA                                        350    AGCAACAACC AACTAGAGTG AAAAATACAC ATTGTTCTCT AGACATACAA                                        400    AATTGAGAAA AGAATCTCAA AATTTAGAGA AACAAATCTG AATTTCTAGA                                        450    AGAAAAAAAT AATTATGCAC TTTGCTATTG CTCGAAAAAT AAATGAAAGA                                        500    AATTAGACTT TTTTAAAAGA TGTTAGACTA GATATACTCA AAAGCTATTA                                        550    AAGGAGTAAT ATTCTTCTTA CATTAAGTAT TTTAGTTACA GTCCTGTAAT                                        600    TAAAGACACA TTTTAGATTG TATCTAAACT TAAATGTATC TAGAATACAT                                        650    ATATTTGAAT GCATCATATA CATGTATCCG ACACACCAAT TCTCATAAAA                                        700    AACGTAATAT CCTAAACTAA TTTATCCTTC AAGTCAACTT AAGCCCAATA                                        750    TACATTTTCA TCTCTAAAGG CCCAAGTGGC ACAAAATGTC AGGCCCAATT                                        800    ACGAAGAAAA GGGCTTGTAA AACCCTAATA AAGTGGCACT GGCAGAGCTT                                        850    ACACTCTCAT TCCATCAACA AAGAAACCCT AAAAGCCGCA GCGCCACTGA                                        900    TTTCTCTCCT CCAGGCGAAG ATG CAG ATC TTC GTG AAG ACC TTA                                        944                         Met Gln Ile Phe Val Lys Thr Leu                         1                5    ACG GGG AAG ACG ATC ACC CTA GAG GTT GAG TCT TCC GAC ACC                                        986    Thr Gly Lys Thr Ile Thr Leu Glu Val Glu Ser Ser Asp Thr        10                  15                  20    ATC GAC AAT GTC AAA GCC AAG ATC CAG GAC AAG GAA GGG ATT                                        1028    Ile Asp Asn Val Lys Ala Lys Ile Gln Asp Lys Glu Gly Ile            25                  30                   35    CCC CCA GAC CAG CAG CGT TTG ATT TTC GCC GGA AAG CAG CTT                                        1070    Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gly Lys Gln Leu                40                  45                  50    GAG GAT GGT CGT ACT CTT GCC GAC TAC AAC ATC°CAG AAG GAG                                        1112    Glu Asp Gly Arg Thr Leu Ala Asp Tyr Asn Ile Gln Lys Glu                    55                  60    TCA ACT CTC CAT CTC GTG CTC CGT CTC CGT GGT GGT                                        1148    Ser Thr Leu His Leu Val Leu Arg Leu Arg Gly Gly    65                  70                  75    GGA TCC GCT GTT AAA AGA GTG GGT CGT AGG TTG AAA AAG TTG                                        1190    Gly Ser Ala Val Lys Arg Val Gly Arg Arg Leu Lys Lys Leu                80                  85                  90    GAC CGT AAG ATT GAT AGG TTA GGA GTT GAT TTT TGATC                                        1228    Asp Arg Lys Ile Asp Arg Leu Gly Val Asp Phe                    95                  100    SEQ ID NO. 93    CCAAAGCACA TACTTATCGA TTTAAATTTC ATCGAAGAGA TTAATATCGA                                        50    ATAATCATAT ACATACTTTA AATACATAAC AAATTTTAAA TACATATATC                                        100    TGGTATATAA TTAATTTTTT AAAGTCATGA AGTATGTATC AAATACACAT                                        150    ATGGAAAAAA TTAACTATTC ATAATTTAAA AAATAGAAAA GATACATCTA                                        200    GTGAAATTAG GTGCATGTAT CAAATACATT AGGAAAAGGG CATATATCTT                                        250    GATCTAGATA ATTAACGATT TTGATTTATG TATAATTTCC AAATGAAGGT                                        300    TTATATCTAC TTCAGAAATA ACAATATACT TTTATCAGAA CATTCAACAA                                        350    AGCAACAACC AACTAGAGTG AAAAATACAC ATTGTTCTCT AGACATACAA                                        400    AATTGAGAAA AGAATCTCAA AATTTAGAGA AACAAATCTG AATTTCTAGA                                        450    AGAAAAAAAT AATTATGCAC TTTGCTATTG CTCGAAAAAT AAATGAAAGA                                        500    AATTAGACTT TTTTAAAAGA TGTTAGACTA GATATACTCA AAAGCTATTA                                        550    AAGGAGTAAT ATTCTTCTTA CATTAAGTAT TTTAGTTACA GTCCTGTAAT                                        600    TAAAGACACA TTTTAGATTG TATCTAAACT TAAATGTATC TAGAATACAT                                        650    ATATTTGAAT GCATCATATA CATGTATCCG ACACACCAAT TCTCATAAAA                                        700    AACGTAATAT CCTAAACTAA TTTATCCTTC AAGTCAACTT AAGCCCAATA                                        750    TACATTTTCA TCTCTAAAGG CCCAAGTGGC ACAAAATGTC AGGCCCAATT                                        800    ACGAAGAAAA GGGCTTGTAA AACCCTAATA AAGTGGCACT GGCAGAGCTT                                        850    ACACTCTCAT TCCATCAACA AAGAAACCCT AAAAGCCGCA GCGCCACTGA                                        900    TTTCTCTCCT CCAGGCGAAG ATG CAG ATC TTC GTG AAG ACC TTA                                        944                          Met Gln Ile Phe Val Lys Thr Leu                          1               5    ACG GGG AAG ACG ATC ACC CTA GAG GTT GAG TCT TCC GAC ACC                                        986    Thr Gly Lys Thr Ile Thr Leu Glu Val Glu Ser Ser Asp Thr        10                  15                  20    ATC GAC AAT GTC AAA GCC AAG ATC CAG GAC AAG GAA GGG ATT                                        1028    Ile Asp Asn Val Lys Ala Lys Ile Gln Asp Lys Glu Gly Ile            25                  30                   35    CCC CCA GAC CAG CAG CGT TTG ATT TTC GCC GGA AAG CAG CTT                                        1070    Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gly Lys Gln Leu                40                  45                  50    GAG GAT GGT CGT ACT CTT GCC GAC TAC AAC ATC CAG AAG GAG                                        1112    Glu Asp Gly Arg Thr Leu Ala Asp Tyr Asn Ile Gln Lys Glu                40                  45                  50    TCA ACT CTC CAT CTC GTG CTC CGT CTC CGT GGT GGT GGA TCC                                        1154    Ser Thr Leu His Leu Val Leu Arg Leu Arg Gly Gly Gly Ser    65                  70                  75    __________________________________________________________________________

EXAMPLE 3 Construction of Ubiquitin-lytic Peptide Fusion Plasmids WithPolyubiquitin Promoter and Intron (Ubi7)

Exemplary and preferred pUC19 and pCGN1547 plasmid vectors containing apotato (Solanum tuberosum) polyubiquitin promoter and intron (Ubi7), aregion coding for a ubiquitin polypeptide, and a gene coding for a lyticpeptide are constructed.

To obtain the genomic clone containing a polyubiquitin promoter, intronand ubiquitin polypeptide coding region, a λFIXII potato genomic librarywas first prescreened using PCR as described in Example 2 above. The PCRprimers are homologous to regions of the polyubiquitin cDNA (seeGarbarino J., et al., Plant Molecular Biology 20: 235(1992)). A primerhomologous to the 5' untranslated region of ubiquitin in thepolyubiquitin cDNA and a primer complementary to the amino terminus ofthe ubiquitin coding region in the polyubiquitin cDNA are used. Agenomic clone containing both the polyubiquitin promoter region, intron,and the polyubiquitin coding region was identified.

A chimeric gene is then constructed with a portion of the potatopolyubiquitin genomic clone ligated to a lytic peptide gene, asdescribed in Example 2. PCR is used to generate the Ubi7-ubiquitinportion of the chimeric gene. The Ubi7 promoter region includes the 1220bp promoter and 568 bp intron upstream of the ubiquitin ATG, and theubiquitin polypeptide coding region is 328 bp plus 6 bp of a BamHIrestriction site (SEQ ID NO. 96). This plasmid is designated pUCUbi7.

A nucleotide fragment coding for the lytic peptide corresponding to theamino acid sequence SEQ ID NO. 98) is generated as described in Example2. The resulting Ubi7 ubiquitin-lytic peptide fusion gene constructcorresponds to SEQ ID NO. 95. Unlike previous cloning attempts using theCaMV35S promoter as described in the Background section, the sequencedoes not reveal any point mutations in the lytic peptide sub-clones. Theplasmid was stable in the E. coli host and did not inhibit its growth.

The resulting pUC19 recombinant plasmid is shown in the plasmid map inFIG. 2. The sequence for the PCR insert containing the polyubiquitinpromoter, intron, and the ubiquitin coding region corresponds to SEQ IDNO. 96 in Table 3 below. The sequence for the chimeric Ubi7ubiquitin-lytic peptide fusion gene construct corresponds to SEQ ID NO.95 in Table 3 below. This plasmid is designated as pUCUbi7-LP98.

The entire Ubi7 ubiquitin-lytic peptide fusion gene construct, includingthe polyadenylation site, is isolated from pUC19 as an Asp78/partialHindIII: restriction fragment (the intron has an internal HindIII site)and sub-cloned into the pCGN1547 Agrobacterium vector for use in planttransformation. This plasmid is designated pCGNUbi7-LP98.

                                      TABLE 3    __________________________________________________________________________    NUCLEOTIDE SEQUENCE OF POTATO POLYUBIQUITIN PROMOTER    REGION (UB17) AND UBIQUITIN CODING REGION INSERT,    AND UBIQUITIN-LYTIC PRPTIDE FUSION GENE CONSTRUCT    __________________________________________________________________________    SEQ ID NO. 95    TTTATCAATC AGATTTGAAC ATATAAATAA ATATAAATTG TCTCAATAAT                                        50    TCTACATTAA ACTAATATTT GAAATCTCAA TTTTATGATT TTTTAAATTC                                        100    ACTTTATATC CAAGACAATT TNCANCTTCA AAAAGTTTTA TTAAANATTT                                        150    ACATTAGTTT TGTTGATGAG GATGACAAGA TNTTGGTCAT CAATTACATA                                        200    TACCCAAATT GAATAGTAAG CAACTTCAAT CTTTTTCATA ATGATAATGA                                        250    CAGACACAAN NNAAACCCAT TTATTATTCA CATTGATTGA GTTTTATATG                                        300    CAATATAGTA ATAATAATAA TATTTCTTAT AAAGCAAGAG GTCAATTTTT                                        350    TTTTAATTAT ACCACGTCAC TAAATTATAT TTGATAATGT AAAACAATTC                                        400    AAATTTTACT TAAATATCAT GAAATAAACT ATTTTTATAA CCAAATTACT                                        450    AAATTTTTCC AATAAAAAAA AGTCATTAAG AAGACATAAA ATAAATTTGA                                        500    GGTAAANGAG TGAAGTCGAC TGACTTTTTT TTTTTTTATC ATAAGAAAAT                                        550    AAATTATTAA CTTTAACCTA ATAAAACACT AATATAATTT CATGGAATCT                                        600    AATACTTACC TCTTAGAAAT AAGAAAAAGT GTTTCTAATA GACCCTCAAT                                        650    TTACATTAAA TATTTTCAAT CAAATTTAAA TAACAAATAT CAATATGAGG                                        700    TCAATAACAA TATCAAAATA ATATGAAAAA AGAGCAATAC ATAATATAAG                                        750    GGACGATTTA AGTGCGATTA TCAAGGTAGT ATTATATCCT AATTTGCTAA                                        800    TATTTGNGCT CTTATATTTA AGGTCATGTT CATGATAAAC TTGAAATGCG                                        850    CTATATTAGA GCATATATTA AAATAAAAAA ATACCTAAAA TAAAATTAAG                                        900    TTATTTTTAG TATATATTTT TTTACATGAC CTACATTTTT CTGGGTTTTT                                        950    CTAAAGGAGC GTGTAAGTGT CGACCTCATT CTCCTAATTT TCCCCACCAC                                        1000    ATAAAAATTA AAAAGGAAAG GTAGCTTTTG CGTGTTGTTT TGGTACACTA                                        1050    CACCTCATTA TTACACGTGT CCTCATATAA TTGGTTAACC CTATGAGGCG                                        1100    GTTTCGTCTA GAGTCGGCCA TGCCATCTAT AAAATGAAGC TTTCTGCACC                                        1150    TCATTTTTTT CATCTTCTAT CTGATTTCTA TTATAATTTC TCTCAATTGC                                        1200    CTTCAAATTT CTCTTTAAGG TTAGAATCTT CTCTATTTTT                                        1240    GGTTTTTGTA TGTTTAGATT CTCGAATTAG CTAATCAGGC GCTGTTATAG                                        1290    CCCTTCCTTT TGAGTCTCTC CTCGGTTGTC TTGATGGAAA AGGCCTAACA                                        1340    TTTGAGTTTT TTTACGTCTG GTTTGATGGA AAAGGCCTAC AATTGGCCGT                                        1390    TTTCCCCGTT CGTTTTGATG AAAAAGCCCC TAGTTTGAGA TTTTTTTTCT                                        1440    GTCGTTCGTT CTAAAGGTTT AAAATTAGAG TTTTTACATT TGTTTGATGA                                        1490    AAAAGGCCTT AAATTTGAGT TTTTCCGGTT GATTTGATGA AAAAGCCCTA                                        1540    GAATTTGTGT TTTTCCGTCG GTTTGATTCT GAAGGCCTAA AATTTGAGTT                                        1590    TCTCCGGCTG TTTTGATGAA AAAGCCCTAA ATTTGAGTTT CTCCGGCTGT                                        1640    TTTGATGAAA AAGCCCTAAA TTTGAAGTTT TTTCCCCGTG TTTTAGATTG                                        1690    TTTAGGTTTT AATTCTCGAA TCAGCTAATC AGGGAGTGTG AAAGCCCTAA                                        1740    ATTGAAGTTT TTTTCGTTGT TCTGATTGTT GTTTTTATGA ATTTGCAG                                        1788    ATG CAG ATC TTT GTG AAA ACT CTC ACC GGA AAG ACT ATC ACC                                        1830    Met Gln Ile Phe Val Lys Thr Leu Thr Gly Lys Thr Ile Thr     1               5                  10    CTA GAG GTG GAA AGT TCT GAT ACA ATC GAC AAC GTT AAG GCT                                        1872    Leu Glu Val Glu Ser Ser Asp Thr Ile Asp Asn Val Lys Ala    15                  20                  25    AAG ATC CAG GAT AAG GAA GGA ATT CCC CCG GAT CAG CAA AGG                                        1914    Lys Ile Glu Asp Lys Glu Gly Ile Pro Pro Asp Gln Gln Arg        30                  35                  40    CTT ATC TTC GCC GGA AAG CAG TTG GAG GAC GGA CGT ACT CTA                                        1956    Leu Ile Phe Ala Gly Lys Gln Leu Glu Asp Gly Arg Thr Leu            45                  50                  55    GCT GAT TAC AAC ATC CAG AAG GAG TCT ACC CTC CAT TTG GTG                                        1998    Ala Asp Tyr Asn Ile Gln Lys Glu Ser Thr Leu His Leu Val    CTC CGT CTA CGT GGA GGT GGA TCC GCT GTT AAA AGA GTG GGT -                                        2040    Leu Arg Leu Arg Gly Gly Gly Ser Ala Val Lys Arg Val Gly                    75                    80    CGT AGG TTG AAA AAG TTG GAC CGT AAG ATT GAT AGG TTA GGA                                        2082    Arg Arg Leu Lys Lys Leu Asp Arg Lys Ile Asp Arg Leu Gly    85                  90                  95    GTT GAT TTT TGATCTAGAG CCCCGAATTT CCCCGA                                        2127    Val Asp Phe        100    SEQ ID NO 96    TTTATCAATC AGATTTGAAC ATATAAATAA ATATAAATTG TCTCAATAAT                                        50    TCTACATTAA ACTAATATTT GAAATCTCAA TTTTATGATT TTTTAAATTC                                        100    ACTTTATATC CAAGACAATT TNCANCTTCA AAAAGTTTTA TTAAANATTT                                        150    ACATTAGTTT TGTTGATGAG GATGACAAGA TNTTGGTCAT CAATTACATA                                        200    TACCCAAATT GAATAGTAAG CAACTTCAAT GTTTTTCATA ATGATAATGA                                        250    CAGACACAAN NNAAACCCAT TTATTATTCA CATTGATTGA GTTTTATATG                                        300    CAATATAGTA ATAATAATAA TATTTCTTAT AAAGCAAGAG GTCAATTTTT                                        350    TTTTAATTAT ACCACGTCAC TAAATTATAT TTGATAATGT AAAACAATTC                                        400    AAATTTTACT TAAATATCAT GAAATAAACT ATTTTTATAA CCAAATTACT                                        450    AAATTTTTCC AATAAAAAAA AGTCATTAAG AAGACATAAA ATAAATTTGA                                        500    GGTAAANGAG TGAAGTCGAC TGACTTTTTT TTTTTTTATC ATAAGAAAAT                                        550    AAATTATTAA CTTTAACCTA ATAAAACACT AATATAATTT CATGGAATCT                                        600    AATACTTACC TCTTAGAAAT AAGAAAAAGT GTTTCTAATA GACCCTCAAT                                        650    TTACATTAAA TATTTTCAAT CAAATTTAAA TAACAAATAT CAATATGAGG                                        700    TCAATAACAA TATCAAAATA ATATGAAAAA AGAGCAATAC ATAATATAAG                                        750    GGACGATTTA AGTGCGATTA TCAAGGTAGT ATTATATCCT AATTTGCTAA                                        800    TATTTGNGCT CTTATATTTA AGGTCATGTT CATGATAAAC TTGAAATGCG                                        850    CTATATTAGA GCATATATTA AAATAAAAAA ATACCTAAAA TAAAATTAAG                                        900    TTATTTTTAG TATATATTTT TTTACATGAC CTACATTTTT CTGGGTTTTT                                        950    CTAAAGGAGC GTGTAAGTGT CGACCTCATT CTCCTAATTT TCCCCACCAC                                        1000    ATAAAAATTA AAAAGGAAAG GTAGCTTTTG CGTGTTGTTT TGGTACACTA                                        1050    CACCTCATTA TTACACGTGT CCTCATATAA TTGGTTAACC CTATGAGGCG                                        1100    GTTTCGTCTA GAGTCGGCCA TGCCATCTAT AAAATGAAGC TTTCTGCACC                                        1150    TCATTTTTTT CATCTTCTAT CTGATTTCTA TTATAATTTC TCTCAATTGC                                        1200    CTTCAAATTT CTCTTTAAGG TTAGAATCTT CTCTATTTTT                                        1240    GGTTTTTGTA TGTTTAGATT CTCGAATTAG CTAATCAGGC GCTGTTATAG                                        1290    CCCTTCCTTT TGAGTCTCTC CTCGGTTGTC TTGATGGAAA AGGCCTAACA                                        1340    TTTGAGTTTT TTTACGTCTG GTTTGATGGA AAAGGCCTAC AATTGGCCGT                                        1390    TTTCCCCGTT CGTTTTGATG AAAAAGCCCC TAGTTTGAGA TTTTTTTTCT                                        1440    GTCGTTCGTT CTAAAGGTTT AAAATTAGAG TTTTTACATT TGTTTGATGA                                        1490    AAAAGGCCTT AAATTTGAGT TTTTCCGGTT GATTTGATGA AAAAGCCCTA                                        1540    GAATTTGTGT TTTTCCGTCG GTTTGATTCT GAAGGCCTAA AATTTGAGTT                                        1590    TCTCCGGCTG TTTTGATGAA AAAGCCCTAA ATTTGAGTTT CTCCGGCTGT                                        1640    TTTGATGAAA AAGCCCTAAA TTTGAAGTTT TTTCCCCGTG TTTTAGATTG                                        1690    TTTAGGTTTT AATTCTCGAA TCAGCTAATC AGGGAGTGTG AAAGCCCTAA                                        1740    ATTGAAGTTT TTTTCGTTGT TCTGATTGTT GTTTTTATGA ATTTGCAG                                        1788    ATG CAG ATC TTT GTG AAA ACT CTC ACC GGA AAG ACT ATC ACC                                        1830    Met Gln Ile Phe Val Lys Thr Leu Thr Gly Lys Thr Ile Thr     1               5                  10    CTA GAG GTG GAA AGT TCT GAT ACA ATC GAC AAC GTT AAG GCT                                        1872    Leu Glu Val Glu Ser Ser Asp Thr Ile Asp Asn Val Lys Ala    15                  20                  25    AAG ATC CAG GAT AAG GAA GGA ATT CCC CCG GAT CAG CAA AGG                                        1914    Lys Ile Glu Asp Lys Glu Gly Ile Pro Pro Asp Gln Gln Arg        30                  35                  40    CTT ATC TTC GCC GGA AAG CAG TTG GAG GAC GGA CGT ACT CTA                                        1956    Leu Ile Phe Ala Gly Lys Gln Leu Glu Asp Gly Arg Thr Leu            45                  50                  55    GCT GAT TAC AAC ATC CAG AAG GAG TCT ACC CTC CAT TTG GTG                                        1998    Ala Asp Tyr Asn Ile Gln Lys Glu Ser Thr Leu His Leu Val                60                  65                  70    CTC CGT CTA CGT GGA GGT GGA TCC     2022    Leu Arg Leu Arg Gly Gly Gly Ser                    75    __________________________________________________________________________

EXAMPLE 4 Construction of Ubiquitin-Lytic Peptide Fusion Gene PlasmidVectors

pUC19 and pCGN1547 plasmid vectors containing a potato (Solanumtuberosum) Ubi3 promoter, a region coding for a ubiquitin polypeptide,and a gene coding for a lytic peptide are constructed according toExample 2. Each plasmid respectively contains one lytic peptidenucleotide sequence coding for an amino acid sequence corresponding toSEQ ID NO. 1, 7, 15, 21, 30, 39, 43, 52, 83, 86, 88, 90, and 91. Theresultant pUC19 Ubi3 ubiquitin-lytic peptide recombinant plasmids aredesignated as follows: pUCUbi3-LP1, pUCUbi3-LP7, pUCUbi3-LP15,pUCUbi3-LP21, pUCUbi3-LP30, pUCUbi3-LP39, pUCUbi3-LP43, pUCUbi3-LP52,pUCUbi3-LP83, pUCUbi3-LP86, pUCUbi3-LP88, pUCUbi3-LP90, andpUCUbi3-LP91. The resultant pCGN1547 Ubi3 ubiquitin-lytic peptiderecombinant plasmids are designated as follows: pCGNUbi3-LP1,pCGNUbi3-LP7, pCGNUbi3-LP15, pCGNUbi3-LP21, pCGNUbi3-LP30,pCGNUbi3-LP39, pCGNUbi3-LP43, pCGNUbi3-LP52, pCGNUbi3-LP83,pCGNUbi3-LP86, pCGNUbi3-LP88, pCGNUbi3-LP90, and pCGNUbi3-LP91.

pUC19 and pCGN1547 plasmid vectors containing a potato (Solanumtuberosum) Ubi7 promoter and intron, a region coding for a ubiquitinpolypeptide, and a gene coding for a lytic peptide are constructedaccording to Example 3. Each plasmid respectively contains one lyticpeptide nucleotide sequence coding for an amino acid sequencecorresponding to SEQ ID NO. 1, 7, 15, 21, 30, 39, 43, 52, 83, 86, 88,90, and 91. The resultant pUC19 Ubi7 ubiquitin-lytic peptide recombinantplasmids are designated as follows: pUCUbi7-LP1, pUCUbi7-LP7,pUCUbi7-LP15, pUCUbi7-LP21, pUCUbi7-LP30, pUCUbi7-P39, pUCUbi7-LP43,pUCUbi7-LP52, pUCUbi7-LP83, pUCUbi7-LP86, pUCUbi7-LP88, pUCUbi7-LP90,and pUCUbi7-LP91. The resultant pCGN1547 Ubi7 ubiquitin-lytic peptiderecombinant plasmids are designated as follows: pCGNUbi7-LP1,pCGNUbi7-LP7, pCGNUbi7-LP15, pCGNUbi7,-LP21, pCGNUbi7-LP30,pCGNUbi7-LP39, pCGNUbi7-LP43, pCGNUbi7-LP52, pCGNUbi7-LP83,pCGNUbi7-LP86, pCGNUbi7-LP88, pCGNUbi7-LP90, and pCGNUbi7-LP91.

EXAMPLE 5 Construction of GUS-Ubiquitin Fusion Gene Recombinant DNAMolecules and Ubiquitin Promoter-GUS Recombinant DNA Molecules

Two chimeric genes containing a β-glucuronidase (GUS) reporter gene andthe Ubi3 promoter were constructed in-pCGN1547 plasmid vectors accordingto Garbarino, J., and Belknap, W., Plant Molecular Biology 24: 119(1994), hereby incorporated by reference in its entirety. The firstvector contains the 920 bp Ubi3 promoter ligated to the GUS gene, andexpresses the GUS protein. This plasmid is designated pCGNUbi3-GUS. Thesecond vector contains the 920 bp Ubi3 promoter and 228 bp ubiquitincoding region ligated in frame to the GUS gene. This plasmid expresses aubiquitin-GUS fusion polypeptide. This plasmid is designatedpCGNUbi3-GUSf.

Two chimeric genes containing a β-glucuronidase (GUS) reporter gene andthe Ubi7 promoter minus the intron region were constructed in pCGN1547plasmid vectors using PCR, as described in Example 3 and in Garbarino,J., and Belknap, W., Plant Molecular Biology 24: 119 (1994). The firstvector contains a 1156 bp Ubi7 promoter region insert, including she 5'untranslated region of ubiquitin, ligated to the GUS gene. This plasmiddoes not contain the Ubi7 intron and expresses the GUS protein. Thisplasmid is designated pCGNUbi7-GUS. The second vector contains the 1156Ubi7 ubiquitin promoter from pCGNUbi7-GUS and the 228 bp ubiquitincoding region fused in frame to the GUS reporter gene. This plasmidexpresses a ubiquitin-GUS fusion polypeptide and is designatedpCGNUbi7-GUSf.

EXAMPLE 6 Plant Transformation and GUS Gene Expression

The chimeric plasmids pCGNUbi3-GUS, pCGNUbi3-GUSf, pCGNUbi7-GUS, andpCGNUbi7-GUSf from Example 5 are introduced into the potato (Solanumtuberosum) using Agrobacterium mediated transformation according toGarbarino, J., and Belknap, W. Plant Molecular Biology 24:119 (1994).The strain of Agrobacterium tumefaciens used for transformation (PC2760,see An, G., et al., EMBO J. 4: 277 (1985)) harbors the disarmed Tiplasmid pAL4404 (see Hoekema, A., et al., Nature 303: 179 (1983). Planttransformation is carried out as previously described in Synder, G. W.,et al., Plant Cell Rep 12:324 (1993), except that 1 mg/l silverthiosulfate is added to the stage II transformation medium (see Chang,H. H., et al., Bot Bull Acad Sci 32: 63 (1991).

Expression of the ubiquitin-GUS fusion polypeptide and MRNA products andthe GUS protein alone is examined by northern and western analysis, asdescribed in Garbarino J., and Belknap, W., Plant Molecular Biology 24:119 (1994). GUS protein expression is examined in the transgenic plantsusing western analysis. Although there is a wide range of activity amongindividual clones, the ubiquitin-GUS fusion polypeptide containingplants generally give 5-10 fold higher expression than the plantscontaining GUS protein alone. This higher level of protein expressionCorresponds to similarly elevated mRNA transcription levels for theubiquitin-GUS fusion constructs, as shown by northern analysis(described in Garbarino et al., Plant Molecular Biology 24: 119 (1994)).Western analysis also shows that the ubiquitin-GUS fusion polypeptidewas appropriately processed by endogenous ubiquitin hydrolases coproduce free GUS protein.

GUS protein activity is measured as described by Jefferson, R. A., etal., EMBO J. 6: 3901 (1987). Table 4 below shows a comparison of the GUSactivities in plants transformed with pCGNUbi3-GUS (ubi-) and plantstransformed with pCGNUbi3-GUSf (ubi+). The activity is measured innmoles methyl umbelliferon (MU) per minute per milligram of protein.Methyl umbelliferon is the fluorescent product of the GUS enzymaticreaction.

                  TABLE 4    ______________________________________    COMPARISON OF GUS PROTEIN ACTIVITY IN PLANTS    TRANSFORMED WITH THE UBI3 PROMOTER WITH (+UBI)    AND WITHOUT (-UBI) UBIQUITIN POLYPEPTIDE FUSION    GUS Activity (nmoles MU/min/mg protein)            Leaf                     Senescent    Construct            Meristem 2nd Leaf 5th Leaf                                     Leaf   Tuber    ______________________________________    3.2 - ubi            6.31 ±                     2.51 ±                              1.79 ±                                      5.42 ±                                            3.26 ±            0.74     0.52     0.22    1.24  0.27    8.1 - ubi            25.8 ±                     9.98 ±                              6.34 ±                                     19.20 ±                                            14.2 ±            2.08     2.10     1.00    6.11   1.6    3.5 + ubi            94.8 ±                     60.3 ±                              32.7 ±                                      50.1 ±                                            37.6 ±            12.6     25.1     8.71    11.6  10.4    9.8 + ubi            33.3 ±                     18.9 ±                              9.74 ±                                      22.7 ±                                            20.7 ±             0.5     2.75     0.99    3.57  3.45    ______________________________________

EXAMPLE 7 Plant Transformation and Ubiquitin-Lytic Peptide GeneExpression

The chimeric plasmids pCGNUbi3-LP98 from Example 2 and pCGNUbi7-LP98from Example 3 are introduced into the potato (Solanum tuberosum) usingAgrobacterium mediated transformation according to Garbarino, J., andBelknap, W. Plant Molecular Biology 24:119 (1994). The strain ofAgrobacterium tumefaciens used for transformation (PC2760, see An, G.,et al., 3EMBO J. 4: 277 (1985)) harbors the disarmed Ti plasmid pAL4404(see Hoekema, A., et al., Nature 303: 179 (1983). Plant transformationis carried out as previously described in Synder, G. W., et al., PlantCell Rep 12:324 (1993), except that 1 mg/l silver thiosulfate is addedto the stage II transformation medium (see Chang, H. H., et al., BotBull Acad Sci 32: 63 (1991).

Expression of the ubiquitin-lytic peptide fusion polypeptide and mRNAproducts is examined by northern and western analysis, in Garbarino J.,and Belknap, W., Plant Molecular Biology 24: 119 (1994). Northernanalysis shows that ubiquitin-lytic peptide mRNA is transcribed from thegene construct in the transgenic plants. Western analysis shows that theubiquitin-lytic peptide fusion polypeptide is appropriately processed byendogenous ubiquitin in hydrolases to produce free lytic peptide.

EXAMPLE 8 Cloned Ubi3/Ubi7 Promoter Activity

mRNA expression from the cloned Ubi3 promoter was examined before andafter wounding to determine if the cloned Ubi3 promoter is woundinducible in transformed plants (see Garbarino, J. and Belknap, W.,Plant Molecular Biology 24:119 (1994)). Northern analysis comparingendogenous Ubi3 mRNA expression levels to pCGNUbi3-GUS and pCGNUbi3-GUSfmRNA expression levels in transformed plants (see Example 5) shows thatwhile the endogenous Ubi3 mRNA transcription increases upon wounding,transcription from the recombinant Ubi3 plasmids does not. Thus therecombinant Ubi3 promoter does not have the wound induciblecharacteristic of the endogenous Ubi3 promoter. This result suggeststhat the 920 bp of upstream sequence cloned in the Ubi3 genomic clone isnot sufficient to obtain wound-dependent activation of the promoter. Thepromoter instead is constitutive, however, it still demonstratesdevelopmental regulation, as shown in Table 4 above.

In contrast, the cloned TUi-b promoter retains its wound-dependentinduction. Northern analysis comparing the endogenous Ubi7 mRNAexpression levels to the expression levels from pCGNUbi7-GUS andpCGNUbi7-GUSf in transformed plants (see Example 5) shows that both theendogenous and the cloned Ubi7 promoter have wound-dependent activation.

DEPOSIT INFORMATION

E. coli cultures, each respectively transformed with pUCUbi7-LP98 (LocalAccession No. PBT-0273), pUCUbi3-LP98 (Local Accession No. PBT-0276),pUCUbi7 (Local Accession No. PBT-0277), and pUCUbi3 (Local Accession No.PBT-0234) were deposited in the Agricultural Research Service CultureCollection (NRRL). The depository is located at located at 1815 NorthUniversity Street, Peoria, Ill.,

    __________________________________________________________________________    #             SEQUENCE LISTING    - (1) GENERAL INFORMATION:    -    (iii) NUMBER OF SEQUENCES: 98    - (2) INFORMATION FOR SEQ ID NO: 1:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #1:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Lys Ala Val Lys Lys Al - #a Val Lys Lys Val Lys    #                15    - Lys Ala Val Lys Lys Ala Val Lys Lys Lys Ly - #s    #            25    - (2) INFORMATION FOR SEQ ID NO: 2:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 32              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #2:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Lys Ala Val Ala Val Ly - #s Ala Val Lys Lys Ala    #                15    - Val Lys Lys Val Lys Lys Ala Val Lys Lys Al - #a Val Lys Lys Lys Lys    #            30    - (2) INFORMATION FOR SEQ ID NO: 3:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 37              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #3:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Lys Ala Val Ala Val Ly - #s Ala Val Ala Val Lys    #                15    - Ala Val Lys Lys Ala Val Lys Lys Val Lys Ly - #s Ala Val Lys Lys Ala    #            305    - Val Lys Lys Lys Lys            35    - (2) INFORMATION FOR SEQ ID NO: 4:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #4:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Lys Ala Val Lys Lys Al - #a Val Lys Lys Val Lys    #                15    - Lys Ala Val Lys Lys Ala Val                20    - (2) INFORMATION FOR SEQ ID NO: 5:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 28              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #5:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Lys Ala Val Ala Val Ly - #s Ala Val Lys Lys Ala    #                15    - Val Lys Lys Val Lys Lys Ala Val Lys Lys Al - #a Val    #            25    - (2) INFORMATION FOR SEQ ID NO: 6:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 33              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #6:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Lys Ala Val Ala Val Ly - #s Ala Val Ala Val Lys    #                15    - Ala Val Lys Lys Ala Val Lys Lys Val Lys Ly - #s Ala Val Lys Lys Ala    #            305    - Val    - (2) INFORMATION FOR SEQ ID NO: 7:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #7:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Gly Leu Arg Ala Ile Lys Arg Al - #a Leu Lys Lys Leu Arg    #                15    - Arg Gly Val Arg Lys Val Ala Lys Arg Lys Ar - #g    #            25    - (2) INFORMATION FOR SEQ ID NO: 8:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #8:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Gly Leu Arg Ala Ile Lys Arg Al - #a Leu Lys Lys Leu Arg    #                15    - Arg Gly Val Arg Lys Val Ala                20    - (2) INFORMATION FOR SEQ ID NO: 9:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #9:   (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Arg Lys Arg Ala Val Lys Arg Val Gly Ar - #g Arg Leu Lys Lys Leu    #                15    - Ala Arg Lys Ile Ala Arg Leu Gly Val Ala Ph - #e    #             25    - (2) INFORMATION FOR SEQ ID NO: 10:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #10:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Ala Val Lys Arg Val Gly Arg Arg Leu Lys Ly - #s Leu Ala Arg Lys Ile    #                15    - Ala Arg Leu Gly Val Ala Phe                20    - (2) INFORMATION FOR SEQ ID NO: 11:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 31              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    - 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Phe Ala Val Gly Leu Arg Ala Ile Lys Arg Al - #a Leu Lys Lys Leu Arg    #                15    - Arg Gly Val Arg Lys Val Ala Lys Asp Leu    #            25    - (2) INFORMATION FOR SEQ ID NO: 13:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 30              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #13:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Arg Lys Arg Ala Val Lys Arg Val Gly Ar - #g Arg Leu Lys Lys Leu    #                15    - Ala Arg Lys Ile Ala Arg Leu Gly Val Ala Ph - #e Lys Asp Leu    #            30    - (2) INFORMATION FOR SEQ ID NO: 14:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 26              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    - 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Lys Lys Lys Lys Phe Val Lys Lys Val Ala Ly - #s Lys Val Lys Lys Val    #                15    - Ala Lys Lys Val Ala Lys Val Ala Val Ala Va - #l    #            25    - (2) INFORMATION FOR SEQ ID NO: 16:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 32              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #16:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Lys Lys Lys Phe Val Lys Lys Val Ala Ly - #s Lys Val Lys Lys Val    #                15    - Ala Lys Lys Val Ala Lys Val Ala Val Ala Ly - #s Val Ala Val Ala Val    #            305    - (2) INFORMATION FOR SEQ ID NO: 17:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 37              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    - 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Lys Lys Lys Lys Phe Val Lys Lys Val Ala Ly - #s Val Ala Lys Lys Val    #                15    - Ala Lys Val Ala Lys Lys Val Ala Lys Lys Va - #l    #            25    - (2) INFORMATION FOR SEQ ID NO: 22:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 32              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #22:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Lys Lys Lys Phe Val Lys Lys Val Ala Ly - #s Val Ala Lys Lys Val    #                15    - Ala Lys Val Ala Lys Lys Val Ala Lys Lys Va - #l Ala Lys Lys Val Ala    #            30    - (2) INFORMATION FOR SEQ ID NO: 23:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 37              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    - 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Phe Val Lys Lys Val Ala Lys Val Ala Lys Ly - #s Val Ala Lys Val Ala    #                15    - Lys Lys Val Ala Lys Lys Val Lys Lys Lys Ly - #s    #            25    - (2) INFORMATION FOR SEQ ID NO: 28:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 32              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #28:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Val Lys Lys Val Ala Lys Val Ala Lys Ly - #s Val Ala Lys Val Ala    #                15    - Lys Lys Val Ala Lys Lys Val Ala Lys Lys Va - #l Ala Lys Lys Lys Lys    #            305    - (2) INFORMATION FOR SEQ ID NO: 29:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 37              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    - 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#l Lys Ala Lys Val Lys    #                15    - Ala Lys Val Lys Ala Lys Val Lys Ala Lys Va - #l    #            25    - (2) INFORMATION FOR SEQ ID NO: 39:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 25              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #39:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Lys Val Lys Lys Val Ala Lys Lys Va - #l Cys Lys Cys Val Lys    #                15    - Lys Ala Val Lys Lys Val Lys Lys Phe    #            25    - (2) INFORMATION FOR SEQ ID NO: 40:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #40:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Lys Ala Val Lys Lys Al - #a Val Lys Lys Val Lys    #                15    - Lys Ala Val Lys Lys Ala Val Cys Cys Cys Cy - #s    #            25    - (2) INFORMATION FOR SEQ ID NO: 41:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #41:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Cys Cys Cys Cys Phe Val Lys Lys Val Ala Ly - #s Lys Val Lys Lys Val    #                15    - Ala Lys Lys Val Ala Lys Val Ala Val Ala Va - #l    #            25    - (2) INFORMATION FOR SEQ ID NO: 42:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #42:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Lys Ala Val Lys Lys Al - #a Val Lys Lys Val Lys    #                15    - Lys Ala Val Lys Lys Ala Val Ser Ser Ser Se - #r    #            25    - (2) INFORMATION FOR SEQ ID NO: 43:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    - 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#a Leu Lys Lys Leu Lys    #                 15    - Lys Ala Leu Lys Lys Ala Leu                20    - (2) INFORMATION FOR SEQ ID NO: 45:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #45:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Leu Ala Lys Lys Leu Ala Lys Lys Leu Lys Ly - #s Leu Ala Lys Lys Leu    #                150    - Ala Lys Leu Ala Leu Ala Phe                20    - (2) INFORMATION FOR SEQ ID NO: 46:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    - 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Lys Ala Ile Lys Lys Ala Ile                20    - (2) INFORMATION FOR SEQ ID NO: 48:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #48:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Lys Lys Phe Ala Lys Lys Phe Lys Ly - #s Phe Ala Lys Lys Phe    #                150    - Ala Lys Phe Ala Phe Ala Phe                20    - (2) INFORMATION FOR SEQ ID NO: 49:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 17              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #49:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Arg Leu Ala Lys Ile Lys Val Leu Ar - #g Leu Ala Lys Ile Lys    #                150    - Arg    - (2) INFORMATION FOR SEQ ID NO: 50:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 37              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #50:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Leu Lys Leu Ala Val Lys Leu Val Gly Le - #u Leu Arg Lys Lys Arg    #                150    - Ala Leu Lys Ile Ala Leu Arg Gly Val Ala Ly - #s Arg Ala Gly Arg Leu    #            30    - Ala Val Arg Lys Phe            35    - (2) INFORMATION FOR SEQ ID NO: 51:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 26              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #51:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Arg Ala Arg Lys Ala Arg Lys Lys Al - #a Arg Lys Lys Arg Lys    #                150    - Lys Ala Arg Lys Lys Ala Arg Lys Asp Arg    #            25    - (2) INFORMATION FOR SEQ ID NO: 52:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #52:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Cys Ala Val Cys Cys Al - #a Val Cys Cys Val Cys    #                150    - Cys Ala Val Cys Cys Ala Val                20    - (2) INFORMATION FOR SEQ ID NO: 53:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #53:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Ser Ala Val Ser Ser Al - #a Val Ser Ser Val Ser    #                150    - Ser Ala Val Ser Ser Ala Val                20    - (2) INFORMATION FOR SEQ ID NO: 54:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #54:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Val Ala Val Ser Ala Val Ser Ser Al - #a Val Ser Ser Val Ser    #                150    - Ser Ala Val Ser Ser Ala Val Ser Ser Ser Se - #r    #            25    - (2) INFORMATION FOR SEQ ID NO: 55:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #55:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Lys Lys Phe Ala Lys Lys Phe Lys Ly - #s Phe Ala Lys Lys Phe    #                150    - Ala Lys Phe Ala Phe Ala Phe Lys Lys Lys Ly - #s    #            25    - (2) INFORMATION FOR SEQ ID NO: 56:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #56:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Lys Lys Lys Phe Ala Lys Lys Phe Ala Ly - #s Lys Phe Lys Lys Phe    #                150    - Ala Lys Lys Phe Ala Lys Phe Ala Phe Ala Ph - #e    #            25    - (2) INFORMATION FOR SEQ ID NO: 57:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #57:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Ala Arg Lys Phe Leu Lys Arg Phe Lys Ly - #s Phe Val Arg Lys Phe    #                150    - Ile Arg Phe Ala Phe Leu Phe                20    - (2) INFORMATION FOR SEQ ID NO: 58:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    - 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   (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #67:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Arg Lys Arg Phe Lys Leu Arg Ala Lys Il - #e Lys Val Arg Leu Arg    #                150    - Ala Lys Ile Lys Leu                20    - (2) INFORMATION FOR SEQ ID NO: 68:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 21              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #68:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Le - #u Arg Ala Lys Ile Lys    #                150    - Leu Lys Arg Lys Arg                20    - (2) INFORMATION FOR SEQ ID NO: 69:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #69:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Le - #u Arg Ala Lys Ile Lys    #                150    - Leu Arg Val Lys Leu Lys Ile                20    - (2) INFORMATION FOR SEQ ID NO: 70:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #70:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Le - #u Arg Ala Lys Ile Lys    #                150    - Leu Arg Val Lys Leu Lys Ile Lys Arg Lys Ar - #g    #            25    - (2) INFORMATION FOR SEQ ID NO: 71:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #71:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Arg Lys Arg Phe Lys Leu Arg Ala Lys Il - #e Lys Val Arg Leu Arg    #                150    - Ala Lys Ile Lys Leu Arg Val Lys Leu Lys Il - #e    #            25    - (2) INFORMATION FOR SEQ ID NO: 72:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 29              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #72:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Le - #u Arg Ala Lys Ile Lys    #                150    - Leu Arg Val Lys Leu Lys Ile Arg Ala Arg Il - #e Lys Leu    #            25    - (2) INFORMATION FOR SEQ ID NO: 73:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 33              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #73:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Le - #u Arg Ala Lys Ile Lys    #                150    - Leu Arg Val Lys Leu Lys Ile Arg Ala Arg Il - #e Lys Leu Lys Arg Lys    #            30    - Arg    - (2) INFORMATION FOR SEQ ID NO: 74:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 33              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #74:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Arg Lys Arg Phe Lys Leu Arg Ala Lys Il - #e Lys Val Arg Leu Arg    #                150    - Ala Lys Ile Lys Leu Arg Val Lys Leu Lys Il - #e Arg Ala Arg Ile Lys    #            30    - Leu    - (2) INFORMATION FOR SEQ ID NO: 75:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #75:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Le - #u Arg Ala Lys Ile Lys    #                150    - Leu Val Phe Ala Ile Leu Leu                20    - (2) INFORMATION FOR SEQ ID NO: 76:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #76:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Phe Lys Leu Arg Ala Lys Ile Lys Val Arg Le - #u Arg Ala Lys Ile Lys    #                150    - Leu Val Phe Ala Ile Leu Leu Lys Arg Lys Ar - #g    #            25    - (2) INFORMATION FOR SEQ ID NO: 77:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #77:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Arg Lys Arg Phe Lys Leu Arg Ala Lys Il - #e Lys Val Arg Leu Arg    #                150    - Ala Lys Ile Lys Leu Val Phe Ala Ile Leu Le - #u    #            25    - (2) INFORMATION FOR SEQ ID NO: 78:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #78:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Val Phe Ala Ile Leu Leu Phe Lys Leu Arg Al - #a Lys Ile Lys Val Arg    #                150    - Leu Arg Ala Lys Ile Lys Leu                20    - (2) INFORMATION FOR SEQ ID NO: 79:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #79:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Val Phe Ala Ile Leu Leu Phe Lys Leu Arg Al - #a Lys Ile Lys Val Arg    #                150    - Leu Arg Ala Lys Ile Lys Leu Lys Arg Lys Ar - #g    #            25    - (2) INFORMATION FOR SEQ ID NO: 80:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 27              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #80:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Arg Lys Arg Val Phe Ala Ile Leu Leu Ph - #e Lys Leu Arg Ala Lys    #                150    - Ile Lys Val Arg Leu Arg Ala Lys Ile Lys Le - #u    #            25    - (2) INFORMATION FOR SEQ ID NO: 81:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 29              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #81:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Val Gly Glu Cys Val Arg Gly Arg Cys Pro Se - #r Gly Met Cys Cys Ser    #                150    - Gln Phe Gly Tyr Cys Gly Lys Gly Pro Lys Ty - #r Cys Gly    #            25    - (2) INFORMATION FOR SEQ ID NO: 82:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 30              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #82:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Val Gly Glu Cys Val Arg Gly Arg Cys Pro Se - #r Gly Met Cys Cys Ser    #                150    - Gln Phe Gly Tyr Cys Gly Lys Gly Pro Lys Ty - #r Cys Gly Arg    #            30    - (2) INFORMATION FOR SEQ ID NO: 83:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 30              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #83:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Leu Gly Asp Cys Leu Lys Gly Lys Cys Pro Se - #r Gly Met Cys Cys Ser    #                150    - Asn Tyr Gly Phe Cys Gly Arg Gly Pro Arg Ph - #e Cys Gly Lys    #            30    - (2) INFORMATION FOR SEQ ID NO: 84:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 37              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #84:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Gln Cys Ile Gly Asn Gly Gly Arg Cys Asn Gl - #u Asn Val Gly Pro Pro    #                150    - Tyr Cys Cys Ser Gly Phe Cys Leu Arg Gln Pr - #o Gly Gln Gly Tyr Gly    #            30    - Tyr Cys Lys Asn Arg            35    - (2) INFORMATION FOR SEQ ID NO: 85:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 36              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #85:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Cys Ile Gly Asn Gly Gly Arg Cys Asn Glu As - #n Val Gly Pro Pro Tyr    #                150    - Cys Cys Ser Gly Phe Cys Leu Arg Gln Pro As - #n Gln Gly Tyr Gly Val    #            30    - Cys Arg Asn Arg            35    - (2) INFORMATION FOR SEQ ID NO: 86:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 36              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #86:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Cys Ile Gly Gln Gly Gly Lys Cys Gln Asp Gl - #n Leu Gly Pro Pro Phe    #                150    - Cys Cys Ser Gly Tyr Cys Val Lys Asn Pro Gl - #n Asn Gly Phe Gly Leu    #            30    - Cys Lys Gln Lys            35    - (2) INFORMATION FOR SEQ ID NO: 87:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 44              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #87:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Gln Lys Leu Cys Glu Arg Pro Ser Gly Thr Tr - #p Ser Gly Val Cys Gly    #                150    - Asn Asn Asn Ala Cys Lys Asn Gln Cys Ile As - #n Leu Glu Lys Ala Arg    #            30    - His Gly Ser Cys Asn Tyr Val Phe Pro Ala Hi - #s Lys    #        40    - (2) INFORMATION FOR SEQ ID NO: 88:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 44              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #88:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Gln Arg Val Cys Asp Lys Pro Ser Gly Thr Tr - #p Ser Gly Leu Cys Gly    #                150    - Asn Asn Asn Ala Cys Arg Gln Asn Cys Ile Gl - #n Val Asp Arg Ala Lys    #            30    - Lys Gly Ser Cys Gln Phe Leu Tyr Pro Ala Ly - #s Lys    #        40    - (2) INFORMATION FOR SEQ ID NO: 89:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 36              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #89:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Gln Lys Leu Cys Gln Arg Pro Ser Gly Thr Tr - #p Ser Gly Val Cys Gly    #                150    - Asn Asn Asn Ala Cys Lys Asn Gln Cys Ile Ar - #g Leu Glu Lys Ala Arg    #            30    - His Gly Ser Cys            35    - (2) INFORMATION FOR SEQ ID NO: 90:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 36              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #90:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Gln Arg Val Cys Asn Lys Pro Ser Gly Thr Tr - #p Ser Gly Leu Cys Gly    #                150    - Asn Asn Asn Ala Cys Arg Gln Asn Cys Ile Ly - #s Val Asp Arg Ala Lys    #            30    - Lys Gly Ser Cys            35    - (2) INFORMATION FOR SEQ ID NO: 91:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 20              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #91:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Met Leu Glu Glu Leu Phe Glu Glu Met Thr Gl - #u Phe Ile Glu Glu Val    #                150    - Ile Glu Thr Met                20    - (2) INFORMATION FOR SEQ ID NO: 92:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 1228              (B) TYPE: NUCLEIC ACID    #STRANDED (C) STRANDEDNESS: DOUBLE              (D) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:    #DNA AND OTHER NUCLEIC ACIDGENOMIC    #92:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    #              50TATCGA TTTAAATTTC ATCGAAGAGA TTAATATCGA    #             100ACTTTA AATACATAAC AAATTTTAAA TACATATATC    #             150TTTTTT AAAGTCATGA AGTATGTATC AAATACACAT    #             200CTATTC ATAATTTAAA AAATAGAAAA GATACATCTA    #             250ATGTAT CAAATACATT AGGAAAAGGG CATATATCTT    #             300ACGATT TTGATTTATG TATAATTTCC AAATGAAGGT    #             350GAAATA ACAATATACT TTTATCAGAA CATTCAACAA    #             400AGAGTG AAAAATACAC ATTGTTCTCT AGACATACAA    #             450TCTCAA AATTTAGAGA AACAAATCTG AATTTCTAGA    #             500ATGCAC TTTGCTATTG CTCGAAAAAT AAATGAAAGA    #             550AAAAGA TGTTAGACTA GATATACTCA AAAGCTATTA    #             600TTCTTA CATTAAGTAT TTTAGTTACA GTCCTGTAAT    #             650AGATTG TATCTAAACT TAAATGTATC TAGAATACAT    #             700CATATA CATGTATCCG ACACACCAAT TCTCATAAAA    #             750AACTAA TTTATCCTTC AAGTCAACTT AAGCCCAATA    #             800TAAAGG CCCAAGTGGC ACAAAATGTC AGGCCCAATT    #             850TTGTAA AACCCTAATA AAGTGGCACT GGCAGAGCTT    #             900TCAACA AAGAAACCCT AAAAGCCGCA GCGCCACTGA    - TTTCTCTCCT CCAGGCGAAG ATG CAG ATC TTC GTG AAG AC - #C TTA    #944    #    Met Gln Ile Phe Val Lys Thr Leu    #  5 1    - ACG GGG AAG ACG ATC ACC CTA GAG GTT GAG TC - #T TCC GAC ACC    # 986    Thr Gly Lys Thr Ile Thr Leu Glu Val Glu Se - #r Ser Asp Thr    #    20    - ATC GAC AAT GTC AAA GCC AAG ATC CAG GAC AA - #G GAA GGG ATT    #1028    Ile Asp Asn Val Lys Ala Lys Ile Gln Asp Ly - #s Glu Gly Ile    #         35    - CCC CCA GAC CAG CAG CGT TTG ATT TTC GCC GG - #A AAG CAG CTT    #1070    Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gl - #y Lys Gln Leu    #            50    - GAG GAT GGT CGT ACT CTT GCC GAC TAC AAC AT - #C CAG AAG GAG    #1112    Glu Asp Gly Arg Thr Leu Ala Asp Tyr Asn Il - #e Gln Lys Glu    #                60    #     1148CTC CAT CTC GTG CTC CGT CTC CGT GG - #T GGT    Ser Thr Leu His Leu Val Leu Arg Leu Arg Gl - #y Gly    #75    - GGA TCC GCT GTT AAA AGA GTG GGT CGT AGG TT - #G AAA AAG TTG    #1190    Gly Ser Ala Val Lys Arg Val Gly Arg Arg Le - #u Lys Lys Leu    #            90    #   1228T AAG ATT GAT AGG TTA GGA GTT GAT TT - #T TGATC    Asp Arg Lys Ile Asp Arg Leu Gly Val Asp Ph - #e    #                100    - (2) INFORMATION FOR SEQ ID NO: 93:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 1154              (B) TYPE: NUCLEIC ACID    #STRANDED (C) STRANDEDNESS: DOUBLE              (D) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:    #DNA      (A) DESCRIPTION: GENOMIC    #93:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    #              50TATCGA TTTAAATTTC ATCGAAGAGA TTAATATCGA    #             100ACTTTA AATACATAAC AAATTTTAAA TACATATATC    #             150TTTTTT AAAGTCATGA AGTATGTATC AAATACACAT    #             200CTATTC ATAATTTAAA AAATAGAAAA GATACATCTA    #             250ATGTAT CAAATACATT AGGAAAAGGG CATATATCTT    #             300ACGATT TTGATTTATG TATAATTTCC AAATGAAGGT    #             350GAAATA ACAATATACT TTTATCAGAA CATTCAACAA    #             400AGAGTG AAAAATACAC ATTGTTCTCT AGACATACAA    #             450TCTCAA AATTTAGAGA AACAAATCTG AATTTCTAGA    #             500ATGCAC TTTGCTATTG CTCGAAAAAT AAATGAAAGA    #             550AAAAGA TGTTAGACTA GATATACTCA AAAGCTATTA    #             600TTCTTA CATTAAGTAT TTTAGTTACA GTCCTGTAAT    #             650AGATTG TATCTAAACT TAAATGTATC TAGAATACAT    #             700CATATA CATGTATCCG ACACACCAAT TCTCATAAAA    #             750AACTAA TTTATCCTTC AAGTCAACTT AAGCCCAATA    #             800TAAAGG CCCAAGTGGC ACAAAATGTC AGGCCCAATT    #             850TTGTAA AACCCTAATA AAGTGGCACT GGCAGAGCTT    #             900TCAACA AAGAAACCCT AAAAGCCGCA GCGCCACTGA    - TTTCTCTCCT CCAGGCGAAG ATG CAG ATC TTC GTG AAG AC - #C TTA    #944    #    Met Gln Ile Phe Val Lys Thr Leu    #  5 1    - ACG GGG AAG ACG ATC ACC CTA GAG GTT GAG TC - #T TCC GAC ACC    # 986    Thr Gly Lys Thr Ile Thr Leu Glu Val Glu Se - #r Ser Asp Thr    #    20    - ATC GAC AAT GTC AAA GCC AAG ATC CAG GAC AA - #G GAA GGG ATT    #1028    Ile Asp Asn Val Lys Ala Lys Ile Gln Asp Ly - #s Glu Gly Ile    #         35    - CCC CCA GAC CAG CAG CGT TTG ATT TTC GCC GG - #A AAG CAG CTT    #1070    Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gl - #y Lys Gln Leu    #            50    - GAG GAT GGT CGT ACT CTT GCC GAC TAC AAC AT - #C CAG AAG GAG    #1112    Glu Asp Gly Arg Thr Leu Ala Asp Tyr Asn Il - #e Gln Lys Glu    #                60    - TCA ACT CTC CAT CTC GTG CTC CGT CTC CGT GG - #T GGT GGA TCC    #1154    Ser Thr Leu His Leu Val Leu Arg Leu Arg Gl - #y Gly Gly Ser    #75    - (2) INFORMATION FOR SEQ ID NO: 94:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 78              (B) TYPE: AMINO ACID              (D) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    #94:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Met Gln Ile Phe Val Lys Thr Leu     1                5    - Thr Gly Lys Thr Ile Thr Leu Glu Val Glu Se - #r Ser Asp Thr    #    20    - Ile Asp Asn Val Lys Ala Lys Ile Gln Asp Ly - #s Glu Gly Ile    #         35    - Pro Pro Asp Gln Gln Arg Leu Ile Phe Ala Gl - #y Lys Gln Leu    #            50    - Glu Asp Gly Arg Thr Leu Ala Asp Tyr Asn Il - #e Gln Lys Glu    #                60    - Ser Thr Leu His Leu Val Leu Arg Leu Arg Gl - #y Gly Gly Ser    #75    - (2) INFORMATION FOR SEQ ID NO: 95:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 2127              (B) TYPE: NUCLEIC ACID    #STRANDED (C) STRANDEDNESS: DOUBLE              (D) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:    #DNA AND OTHER DNARIPTION: GENOMIC    #95:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    #              50TTGAAC ATATAAATAA ATATAAATTG TCTCAATAAT    #             100ATATTT GAAATCTCAA TTTTATGATT TTTTAAATTC    #             150ACAATT TNCANCTTCA AAAAGTTTTA TTAAANATTT    #             200GATGAG GATGACAAGA TNTTGGTCAT CAATTACATA    #             250AGTAAG CAACTTCAAT GTTTTTCATA ATGATAATGA    #             300ACCCAT TTATTATTCA CATTGATTGA GTTTTATATG    #             350TAATAA TATTTCTTAT AAAGCAAGAG GTCAATTTTT    #             400CGTCAC TAAATTATAT TTGATAATGT AAAACAATTC    #             450TATCAT GAAATAAACT ATTTTTATAA CCAAATTACT    #             500AAAAAA AGTCATTAAG AAGACATAAA ATAAATTTGA    #             550GTCGAC TGACTTTTTT TTTTTTTATC ATAAGAAAAT    #             600AACCTA ATAAAACACT AATATAATTT CATGGAATCT    #             650AGAAAT AAGAAAAAGT GTTTCTAATA GACCCTCAAT    #             700TTCAAT CAAATTTAAA TAACAAATAT CAATATGAGG    #             750AAAATA ATATGAAAAA AGAGCAATAC ATAATATAAG    #             800CGATTA TCAAGGTAGT ATTATATCCT AATTTGCTAA    #             850TATTTA AGGTCATGTT CATGATAAAC TTGAAATGCG    #             900ATATTA AAATAAAAAA ATACCTAAAA TAAAATTAAG    #             950TATTTT TTTACATGAC CTACATTTTT CTGGGTTTTT    #            1000AAGTGT CGACCTCATT CTCCTAATTT TCCCCACCAC    #            1050GGAAAG GTAGCTTTTG CGTGTTGTTT TGGTACACTA    #            1100ACGTGT CCTCATATAA TTGGTTAACC CTATGAGGCG    #            1150CGGCCA TGCCATCTAT AAAATGAAGC TTTCTGCACC    #            1200TTCTAT CTGATTTCTA TTATAATTTC TCTCAATTGC    #  1240            AAGG TTAGAATCTT CTCTATTTTT    #            1290TAGATT CTCGAATTAG CTAATCAGGC GCTGTTATAG    #            1340TCTCTC CTCGGTTGTC TTGATGGAAA AGGCCTAACA    #            1390CGTCTG GTTTGATGGA AAAGGCCTAC AATTGGCCGT    #            1440TTGATG AAAAAGCCCC TAGTTTGAGA TTTTTTTTCT    #            1490AGGTTT AAAATTAGAG TTTTTACATT TGTTTGATGA    #            1540TTGAGT TTTTCCGGTT GATTTGATGA AAAAGCCCTA    #            1590CCGTCG GTTTGATTCT GAAGGCCTAA AATTTGAGTT    #            1640GATGAA AAAGCCCTAA ATTTGAGTTT CTCCGGCTGT    #            1690CCTAAA TTTGAAGTTT TTTCCCCGTG TTTTAGATTG    #            1740CTCGAA TCAGCTAATC AGGGAGTGTG AAAGCCCTAA    #              1788TTGT TCTGATTGTT GTTTTTATGA ATTTGCAG    - ATG CAG ATC TTT GTG AAA ACT CTC ACC GGA AA - #G ACT ATC ACC    #1830    Met Gln Ile Phe Val Lys Thr Leu Thr Gly Ly - #s Thr Ile Thr    #                10    - CTA GAG GTG GAA AGT TCT GAT ACA ATC GAC AA - #C GTT AAG GCT    #1872    Leu Glu Val Glu Ser Ser Asp Thr Ile Asp As - #n Val Lys Ala    #25    - AAG ATC CAG GAT AAG GAA GGA ATT CCC CCG GA - #T CAG CAA AGG    #1914    Lys Ile Glu Asp Lys Glu Gly Ile Pro Pro As - #p Gln Gln Arg    #    40    - CTT ATC TTC GCC GGA AAG CAG TTG GAG GAC GG - #A CGT ACT CTA    #1956    Leu Ile Phe Ala Gly Lys Gln Leu Glu Asp Gl - #y Arg Thr Leu    #         55    - GCT GAT TAC AAC ATC CAG AAG GAG TCT ACC CT - #C CAT TTG GTG    #1998    Ala Asp Tyr Asn Ile Gln Lys Glu Ser Thr Le - #u His Leu Val    #            70    - CTC CGT CTA CGT GGA GGT GGA TCC GCT GTT AA - #A AGA GTG GGT    #2040    Leu Arg Leu Arg Gly Gly Gly Ser Ala Val Ly - #s Arg Val Gly    #                80    - CGT AGG TTG AAA AAG TTG GAC CGT AAG ATT GA - #T AGG TTA GGA    #2082    Arg Arg Leu Lys Lys Leu Asp Arg Lys Ile As - #p Arg Leu Gly    #95    #                2127GAG TCGACCGATC CCCCGAATTT CCCCGA    Val Asp Phe        100    - (2) INFORMATION FOR SEQ ID NO: 96:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 2022              (B) TYPE: NUCLEIC ACID    #STRANDED (C) STRANDEDNESS: DOUBLE              (D) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:    #DNA      (A) DESCRIPTION: GENOMIC    #96:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    #              50TTGAAC ATATAAATAA ATATAAATTG TCTCAATAAT    #             100ATATTT GAAATCTCAA TTTTATGATT TTTTAAATTC    #             150ACAATT TNCANCTTCA AAAAGTTTTA TTAAANATTT    #             200GATGAG GATGACAAGA TNTTGGTCAT CAATTACATA    #             250AGTAAG CAACTTCAAT GTTTTTCATA ATGATAATGA    #             300ACCCAT TTATTATTCA CATTGATTGA GTTTTATATG    #             350TAATAA TATTTCTTAT AAAGCAAGAG GTCAATTTTT    #             400CGTCAC TAAATTATAT TTGATAATGT AAAACAATTC    #             450TATCAT GAAATAAACT ATTTTTATAA CCAAATTACT    #             500AAAAAA AGTCATTAAG AAGACATAAA ATAAATTTGA    #             550GTCGAC TGACTTTTTT TTTTTTTATC ATAAGAAAAT    #             600AACCTA ATAAAACACT AATATAATTT CATGGAATCT    #             650AGAAAT AAGAAAAAGT GTTTCTAATA GACCCTCAAT    #             700TTCAAT CAAATTTAAA TAACAAATAT CAATATGAGG    #             750AAAATA ATATGAAAAA AGAGCAATAC ATAATATAAG    #             800CGATTA TCAAGGTAGT ATTATATCCT AATTTGCTAA    #             850TATTTA AGGTCATGTT CATGATAAAC TTGAAATGCG    #             900ATATTA AAATAAAAAA ATACCTAAAA TAAAATTAAG    #             950TATTTT TTTACATGAC CTACATTTTT CTGGGTTTTT    #            1000AAGTGT CGACCTCATT CTCCTAATTT TCCCCACCAC    #            1050GGAAAG GTAGCTTTTG CGTGTTGTTT TGGTACACTA    #            1100ACGTGT CCTCATATAA TTGGTTAACC CTATGAGGCG    #            1150CGGCCA TGCCATCTAT AAAATGAAGC TTTCTGCACC    #            1200TTCTAT CTGATTTCTA TTATAATTTC TCTCAATTGC    #  1240            AAGG TTAGAATCTT CTCTATTTTT    #            1290TAGATT CTCGAATTAG CTAATCAGGC GCTGTTATAG    #            1340TCTCTC CTCGGTTGTC TTGATGGAAA AGGCCTAACA    #            1390CGTCTG GTTTGATGGA AAAGGCCTAC AATTGGCCGT    #            1440TTGATG AAAAAGCCCC TAGTTTGAGA TTTTTTTTCT    #            1490AGGTTT AAAATTAGAG TTTTTACATT TGTTTGATGA    #            1540TTGAGT TTTTCCGGTT GATTTGATGA AAAAGCCCTA    #            1590CCGTCG GTTTGATTCT GAAGGCCTAA AATTTGAGTT    #            1640GATGAA AAAGCCCTAA ATTTGAGTTT CTCCGGCTGT    #            1690CCTAAA TTTGAAGTTT TTTCCCCGTG TTTTAGATTG    #            1740CTCGAA TCAGCTAATC AGGGAGTGTG AAAGCCCTAA    #              1788TTGT TCTGATTGTT GTTTTTATGA ATTTGCAG    - ATG CAG ATC TTT GTG AAA ACT CTC ACC GGA AA - #G ACT ATC ACC    #1830    Met Gln Ile Phe Val Lys Thr Leu Thr Gly Ly - #s Thr Ile Thr    #                10    - CTA GAG GTG GAA AGT TCT GAT ACA ATC GAC AA - #C GTT AAG GCT    #1872    Leu Glu Val Glu Ser Ser Asp Thr Ile Asp As - #n Val Lys Ala    #25    - AAG ATC CAG GAT AAG GAA GGA ATT CCC CCG GA - #T CAG CAA AGG    #1914    Lys Ile Glu Asp Lys Glu Gly Ile Pro Pro As - #p Gln Gln Arg    #    40    - CTT ATC TTC GCC GGA AAG CAG TTG GAG GAC GG - #A CGT ACT CTA    #1956    Leu Ile Phe Ala Gly Lys Gln Leu Glu Asp Gl - #y Arg Thr Leu    #         55    - GCT GAT TAC AAC ATC CAG AAG GAG TCT ACC CT - #C CAT TTG GTG    #1998    Ala Asp Tyr Asn Ile Gln Lys Glu Ser Thr Le - #u His Leu Val    #            70    #              2022GA GGT GGA TCC    Leu Arg Leu Arg Gly Gly Gly Ser                    75    - (2) INFORMATION FOR SEQ ID NO: 97:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 37              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #97:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Lys Arg Lys Arg Ala Val Lys Arg Val Gly Ar - #g Arg Leu Lys Lys Leu    #                15    - Ala Arg Lys Ile Ala Arg Leu Gly Val Ala Ly - #s Leu Ala Gly Leu Arg    #            305    - Ala Val Leu Lys Phe            35    - (2) INFORMATION FOR SEQ ID NO: 98:    -      (i) SEQUENCE CHARACTERISTICS:              (A) LENGTH: 23              (B) TYPE: AMINO ACID              (C) TOPOLOGY: LINEAR    -     (ii) MOLECULE TYPE:              (A) DESCRIPTION: PEPTIDE    -    (iii) HYPOTHETICAL: NO    -      (v) FRAGMENT TYPE: COMPLETE PEPTIDE    -     (vi) ORIGINAL SOURCE: SYNTHETIC    -    (vii) IMMEDIATE SOURCE: SYNTHETIC    -      (x) PUBLICATION INFORMATION: NOT PREVIOU - #SLY PUBLISHED    #98:  (xi) SEQUENCE DESCRIPTION: SEQ ID NO:    - Ala Val Lys Arg Val Gly Arg Arg Leu Lys Ly - #s Leu Asp Arg Lys Ile    #                 15    - Asp Arg Leu Gly Val Asp Phe                20    __________________________________________________________________________

What is claimed is:
 1. A lytic peptide comprising the amino acidsequence of SEQ ID NO. 97 .
 2. A lytic peptide comprising an amino acidsequence selected from the group consisting of SEQ ID NOS. 48, 55-65. 3.A lytic peptide comprising an amino acid sequence selected from thegroup consisting of SEQ ID NOS. 66-80.
 4. A lytic peptide of claim 2wherein the peptide has the amino acid sequence of SEQ ID NO.
 57. 5. Alytic peptide of claim 3 wherein the peptide has the amino acid sequenceof SEQ ID NO.
 66. 6. A lytic peptide of claim 2 wherein the peptide hasthe amino acid sequence of SEQ ID NO. 48.